{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,26]],"date-time":"2026-04-26T05:19:06Z","timestamp":1777180746277,"version":"3.51.4"},"reference-count":414,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,4,6]],"date-time":"2023-04-06T00:00:00Z","timestamp":1680739200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Instituto Polit\u00e9cnico de Lisboa","award":["IPL\/2021\/ObeCil_ESTeSL"],"award-info":[{"award-number":["IPL\/2021\/ObeCil_ESTeSL"]}]},{"name":"Instituto Polit\u00e9cnico de Lisboa","award":["IPL\/2022\/WintCilGlu_ESTeSL"],"award-info":[{"award-number":["IPL\/2022\/WintCilGlu_ESTeSL"]}]},{"name":"Instituto Polit\u00e9cnico de Lisboa","award":["LA\/P\/0056\/2020"],"award-info":[{"award-number":["LA\/P\/0056\/2020"]}]},{"name":"FCT","award":["IPL\/2021\/ObeCil_ESTeSL"],"award-info":[{"award-number":["IPL\/2021\/ObeCil_ESTeSL"]}]},{"name":"FCT","award":["IPL\/2022\/WintCilGlu_ESTeSL"],"award-info":[{"award-number":["IPL\/2022\/WintCilGlu_ESTeSL"]}]},{"name":"FCT","award":["LA\/P\/0056\/2020"],"award-info":[{"award-number":["LA\/P\/0056\/2020"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biology"],"abstract":"<jats:p>Microtubules (MTs), dynamic polymers of \u03b1\/\u03b2-tubulin heterodimers found in all eukaryotes, are involved in cytoplasm spatial organization, intracellular transport, cell polarity, migration and division, and in cilia biology. MTs functional diversity depends on the differential expression of distinct tubulin isotypes and is amplified by a vast number of different post-translational modifications (PTMs). The addition\/removal of PTMs to \u03b1- or \u03b2-tubulins is catalyzed by specific enzymes and allows combinatory patterns largely enriching the distinct biochemical and biophysical properties of MTs, creating a code read by distinct proteins, including microtubule-associated proteins (MAPs), which allow cellular responses. This review is focused on tubulin-acetylation, whose cellular roles continue to generate debate. We travel through the experimental data pointing to \u03b1-tubulin Lys40 acetylation role as being a MT stabilizer and a typical PTM of long lived MTs, to the most recent data, suggesting that Lys40 acetylation enhances MT flexibility and alters the mechanical properties of MTs, preventing MTs from mechanical aging characterized by structural damage. Additionally, we discuss the regulation of tubulin acetyltransferases\/desacetylases and their impacts on cell physiology. Finally, we analyze how changes in MT acetylation levels have been found to be a general response to stress and how they are associated with several human pathologies.<\/jats:p>","DOI":"10.3390\/biology12040561","type":"journal-article","created":{"date-parts":[[2023,4,6]],"date-time":"2023-04-06T09:26:01Z","timestamp":1680773161000},"page":"561","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0871-9063","authenticated-orcid":false,"given":"Bruno","family":"Carmona","sequence":"first","affiliation":[{"name":"Centro de Qu\u00edmica Estrutural, Institute of Molecular Sciences, Faculdade de Ci\u00eancias, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal"},{"name":"Escola Superior de Tecnologia da Sa\u00fade de Lisboa, Instituto Polit\u00e9cnico de Lisboa, Av. D. Jo\u00e3o II, Lote 4.69.01, 1990-096 Lisboa, Portugal"}]},{"given":"H. Susana","family":"Marinho","sequence":"additional","affiliation":[{"name":"Centro de Qu\u00edmica Estrutural, Institute of Molecular Sciences, Departamento de Qu\u00edmica e Bioqu\u00edmica, Faculdade de Ci\u00eancias, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal"}]},{"given":"Catarina Lopes","family":"Matos","sequence":"additional","affiliation":[{"name":"Centro de Qu\u00edmica Estrutural, Institute of Molecular Sciences, Faculdade de Ci\u00eancias, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2168-0511","authenticated-orcid":false,"given":"Sofia","family":"Nolasco","sequence":"additional","affiliation":[{"name":"Escola Superior de Tecnologia da Sa\u00fade de Lisboa, Instituto Polit\u00e9cnico de Lisboa, Av. D. Jo\u00e3o II, Lote 4.69.01, 1990-096 Lisboa, Portugal"},{"name":"CIISA\u2014Centro de Investiga\u00e7\u00e3o Interdisciplinar em Sanidade Animal, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, Avenida da Universidade T\u00e9cnica, 1300-477 Lisboa, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6180-7041","authenticated-orcid":false,"given":"Helena","family":"Soares","sequence":"additional","affiliation":[{"name":"Centro de Qu\u00edmica Estrutural, Institute of Molecular Sciences, Faculdade de Ci\u00eancias, Universidade de Lisboa, Campo Grande, 1749-016 Lisboa, Portugal"},{"name":"Escola Superior de Tecnologia da Sa\u00fade de Lisboa, Instituto Polit\u00e9cnico de Lisboa, Av. D. Jo\u00e3o II, Lote 4.69.01, 1990-096 Lisboa, Portugal"}]}],"member":"1968","published-online":{"date-parts":[[2023,4,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1093\/jmcb\/mjz060","article-title":"p53 modifications: Exquisite decorations of the powerful guardian","volume":"11","author":"Liu","year":"2019","journal-title":"J. Mol. Cell Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/s41576-022-00468-7","article-title":"Histone post-translational modifications\u2014Cause and consequence of genome function","volume":"23","author":"Burton","year":"2022","journal-title":"Nat. Rev. Genet."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Wloga, D., Joachimiak, E., and Fabczak, H. (2017). Tubulin Post-Translational Modifications and Microtubule Dynamics. Int. J. Mol. Sci., 18.","DOI":"10.3390\/ijms18102207"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/s41580-021-00399-x","article-title":"Regulation of microtubule dynamics, mechanics and function through the growing tip","volume":"22","author":"Gudimchuk","year":"2021","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1515\/bmc.2010.033","article-title":"Revisiting the tubulin folding pathway: New roles in centrosomes and cilia","volume":"1","author":"Tavares","year":"2010","journal-title":"Biomol. Concepts"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0065-3233(01)59003-8","article-title":"Type II chaperonns, prefoldin, and the tubulin-specific chaperones","volume":"59","author":"Cowan","year":"2001","journal-title":"Adv. Protein Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2919","DOI":"10.1016\/j.jmb.2015.04.013","article-title":"The Mechanism and Function of Group II Chaperonins","volume":"427","author":"Lopez","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S0962-8924(97)01168-9","article-title":"The \u03b1- and \u03b2-tubulin folding pathways","volume":"7","author":"Lewis","year":"1997","journal-title":"Trends Cell Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1006\/jsbi.2001.4386","article-title":"Review: Postchaperonin Tubulin Folding Cofactors and Their Role in Microtubule Dynamics","volume":"135","author":"Avila","year":"2001","journal-title":"J. Struct. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.yexcr.2006.09.002","article-title":"Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer dissociation","volume":"313","author":"Kortazar","year":"2007","journal-title":"Exp. Cell Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1007\/s00018-010-0308-8","article-title":"Tubulin chaperone E binds microtubules and proteasomes and protects against misfolded protein stress","volume":"67","author":"Voloshin","year":"2010","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1146\/annurev.cellbio.13.1.83","article-title":"Microtubule Polymerization Dynamics","volume":"13","author":"Desai","year":"1997","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_13","unstructured":"Serna, M., and Zabala, J.C. (2016). eLS, John Wiley & Sons, Ltd."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"950","DOI":"10.3389\/fcell.2021.656273","article-title":"Colchicine Blocks Tubulin Heterodimer Recycling by Tubulin Cofactors TBCA, TBCB, and TBCE","volume":"9","author":"Nolasco","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.devcel.2020.06.008","article-title":"The Tubulin Code in Microtubule Dynamics and Information Encoding","volume":"54","year":"2020","journal-title":"Dev. Cell"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Choi, S. (2016). Encyclopedia of Signaling Molecules, Springer.","DOI":"10.1007\/978-1-4614-6438-9"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/j.devcel.2009.07.010","article-title":"CLIP-170-Dependent Capture of Membrane Organelles by Microtubules Initiates Minus-End Directed Transport","volume":"17","author":"Lomakin","year":"2009","journal-title":"Dev. Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"4029","DOI":"10.1091\/mbc.e11-03-0260","article-title":"Stimulation of the CLIP-170\u2013dependent capture of membrane organelles by microtubules through fine tuning of microtubule assembly dynamics","volume":"22","author":"Lomakin","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"2400","DOI":"10.1091\/mbc.e16-11-0756","article-title":"CENP-F couples cargo to growing and shortening microtubule ends","volume":"28","author":"Kanfer","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"jcs232843","DOI":"10.1242\/jcs.232843","article-title":"Microtubules at focal adhesions\u2014A double-edged sword","volume":"132","author":"Seetharaman","year":"2019","journal-title":"J. Cell Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1083\/jcb.201206050","article-title":"Targeting and transport: How microtubules control focal adhesion dynamics","volume":"198","author":"Stehbens","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_22","first-page":"558","article-title":"CLASPs link focal-adhesion-associated microtubule capture to localized exocytosis and adhesion site turnover","volume":"16","author":"Stehbens","year":"2014","journal-title":"Nature"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"635511","DOI":"10.3389\/fcell.2021.635511","article-title":"Dynamic Microtubule Arrays in Leukocytes and Their Role in Cell Migration and Immune Synapse Formation","volume":"9","author":"Kopf","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.tcb.2020.06.004","article-title":"Cytoskeletal Crosstalk in Cell Migration","volume":"30","author":"Seetharaman","year":"2020","journal-title":"Trends Cell Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1038\/nrm.2015.14","article-title":"The front and rear of collective cell migration","volume":"17","author":"Mayor","year":"2016","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1159\/000324751","article-title":"Role of the Cytoskeleton in Formation and Maintenance of Angiogenic Sprouts","volume":"48","author":"Bayless","year":"2011","journal-title":"J. Vasc. Res."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Hohmann, T., and Dehghani, F. (2019). The Cytoskeleton\u2014A Complex Interacting Meshwork. Cells, 8.","DOI":"10.3390\/cells8040362"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"874","DOI":"10.1038\/nrm2524","article-title":"Organelle positioning and cell polarity","volume":"9","author":"Bornens","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/s10522-010-9305-4","article-title":"Linking cell polarity, aging and rejuvenation","volume":"12","author":"Budovsky","year":"2010","journal-title":"Biogerontology"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1007\/s12263-013-0371-5","article-title":"Cellular polarity in aging: Role of redox regulation and nutrition","volume":"9","author":"Soares","year":"2013","journal-title":"Genes Nutr."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/21688370.2018.1539596","article-title":"The role of microtubules in the regulation of epithelial junctions","volume":"6","author":"Vasileva","year":"2018","journal-title":"Tissue Barriers"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e1900244","DOI":"10.1002\/bies.201900244","article-title":"The Mechanical Role of Microtubules in Tissue Remodeling","volume":"42","author":"Matis","year":"2020","journal-title":"Bioessays"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1038\/s41556-018-0193-1","article-title":"Polarized microtubule dynamics directs cell mechanics and coordinates forces during epithelial morphogenesis","volume":"20","author":"Singh","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1430","DOI":"10.1111\/jth.14544","article-title":"New insights into cytoskeletal remodeling during platelet production","volume":"17","author":"Ghalloussi","year":"2019","journal-title":"J. Thromb. Haemost."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"4076","DOI":"10.1182\/blood-2005-06-2204","article-title":"Differential roles of microtubule assembly and sliding in proplatelet formation by megakaryocytes","volume":"106","author":"Patel","year":"2005","journal-title":"Blood"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1038\/ncomms1838","article-title":"Microtubule and cortical forces determine platelet size during vascular platelet production","volume":"3","author":"Thon","year":"2012","journal-title":"Nat. Commun."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/ncb3370","article-title":"Cilium assembly and disassembly","volume":"18","author":"Dynlacht","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3713","DOI":"10.1083\/jcb.201610039","article-title":"Microtubule stabilization drives 3D centrosome migration to initiate primary ciliogenesis","volume":"216","author":"Pitaval","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1042\/BST0371007","article-title":"Regulation of microtubule dynamic instability","volume":"37","author":"Akhmanova","year":"2009","journal-title":"Biochem. Soc. Trans."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/j.tcb.2019.07.004","article-title":"Microtubule-Associated Proteins: Structuring the Cytoskeleton","volume":"29","author":"Bodakuntla","year":"2019","journal-title":"Trends Cell Biol."},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Kapoor, T.M. (2017). Metaphase Spindle Assembly. Biology, 6.","DOI":"10.3390\/biology6010008"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1242\/jcs.037622","article-title":"A nuclear-envelope bridge positions nuclei and moves chromosomes","volume":"122","author":"Starr","year":"2009","journal-title":"J. Cell Sci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.ceb.2004.12.011","article-title":"Force generation by dynamic microtubules","volume":"17","author":"Dogterom","year":"2005","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S0091-679X(10)97023-4","article-title":"Modeling Microtubule-Mediated Forces and Centrosome Positioning in Caenorhabditis elegans Embryos","volume":"97","author":"Kimura","year":"2010","journal-title":"Methods Cell Biol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1083\/jcb.200305082","article-title":"Centrosome positioning in interphase cells","volume":"162","author":"Burakov","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4418","DOI":"10.1091\/mbc.e10-07-0627","article-title":"Finding the Cell Center by a Balance of Dynein and Myosin Pulling and Microtubule Pushing: A Computational Study","volume":"21","author":"Zhu","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4834","DOI":"10.1091\/mbc.e11-07-0611","article-title":"Effects of dynein on microtubule mechanics and centrosome positioning","volume":"22","author":"Wu","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"848","DOI":"10.1038\/s41567-018-0154-4","article-title":"Physical forces determining the persistency and centring precision of microtubule asters","volume":"14","author":"Tanimoto","year":"2018","journal-title":"Nat. Phys."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1705","DOI":"10.1091\/mbc.E19-01-0034","article-title":"Force balances between interphase centrosomes as revealed by laser ablation","volume":"30","author":"Odell","year":"2019","journal-title":"Mol. Biol. Cell"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1016\/j.cub.2006.06.026","article-title":"Asymmetric Microtubule Pushing Forces in Nuclear Centering","volume":"16","author":"Daga","year":"2006","journal-title":"Curr. Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1083\/jcb.153.2.397","article-title":"A Mechanism for Nuclear Positioning in Fission Yeast Based on Microtubule Pushing","volume":"153","author":"Tran","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1126\/science.1219147","article-title":"Growing Microtubules Push the Oocyte Nucleus to Polarize the Drosophila Dorsal-Ventral Axis","volume":"336","author":"Zhao","year":"2012","journal-title":"Science"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1091\/mbc.e16-06-0395","article-title":"Centrosome centering and decentering by microtubule network rearrangement","volume":"27","author":"Letort","year":"2016","journal-title":"Mol. Biol. Cell"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"19771","DOI":"10.1073\/pnas.0609267103","article-title":"Anisotropy of cell adhesive microenvironment governs cell internal organization and orientation of polarity","volume":"103","author":"Racine","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1083\/jcb.200807179","article-title":"Mammalian end binding proteins control persistent microtubule growth","volume":"184","author":"Komarova","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nrm2369","article-title":"Tracking the ends: A dynamic protein network controls the fate of microtubule tips","volume":"9","author":"Akhmanova","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1111\/j.1600-0854.2006.00400.x","article-title":"Microtubule Plus End: A Hub of Cellular Activities","volume":"7","author":"Lansbergen","year":"2006","journal-title":"Traffic"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.cell.2009.04.065","article-title":"An EB1-Binding Motif Acts as a Microtubule Tip Localization Signal","volume":"138","author":"Honnappa","year":"2009","journal-title":"Cell"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1038\/ncb1703","article-title":"EB1 regulates microtubule dynamics and tubulin sheet closure in vitro","volume":"10","author":"Vitre","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1038\/nature06386","article-title":"Reconstitution of a microtubule plus-end tracking system in vitro","volume":"450","author":"Bieling","year":"2007","journal-title":"Nature"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.cell.2012.02.049","article-title":"EBs Recognize a Nucleotide-Dependent Structural Cap at Growing Microtubule Ends","volume":"149","author":"Maurer","year":"2012","journal-title":"Cell"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.cub.2012.06.068","article-title":"Estimating the Microtubule GTP Cap Size In Vivo","volume":"22","author":"Seetapun","year":"2012","journal-title":"Curr. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/j.cell.2015.07.012","article-title":"Mechanistic Origin of Microtubule Dynamic Instability and Its Modulation by EB Proteins","volume":"162","author":"Zhang","year":"2015","journal-title":"Cell"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"e13470","DOI":"10.7554\/eLife.13470","article-title":"The size of the EB cap determines instantaneous microtubule stability","volume":"5","author":"Duellberg","year":"2016","journal-title":"Elife"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1083\/jcb.200901042","article-title":"GSK3\u03b2 phosphorylation modulates CLASP\u2013microtubule association and lamella microtubule attachment","volume":"184","author":"Kumar","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.devcel.2006.05.012","article-title":"CLASPs Attach Microtubule Plus Ends to the Cell Cortex through a Complex with LL5\u03b2","volume":"11","author":"Lansbergen","year":"2006","journal-title":"Dev. Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1038\/nrm1664","article-title":"CLIPs and CLASPs and cellular dynamics","volume":"6","author":"Galjart","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1146\/annurev-cellbio-101512-122345","article-title":"Microtubule-Depolymerizing Kinesins","volume":"29","author":"Walczak","year":"2013","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/S0955-0674(01)00289-7","article-title":"The oncoprotein 18\/stathmin family of microtubule destabilizers","volume":"14","author":"Cassimeris","year":"2002","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"20449","DOI":"10.1073\/pnas.1309958110","article-title":"Mechanism for the catastrophe-promoting activity of the microtubule destabilizer Op18\/stathmin","volume":"110","author":"Gupta","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1038\/nrm.2017.75","article-title":"Microtubule nucleation: Beyond the template","volume":"18","author":"Roostalu","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/0092-8674(93)90377-3","article-title":"Identification of katanin, an ATPase that severs and disassembles stable microtubules","volume":"75","author":"McNally","year":"1993","journal-title":"Cell"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1083\/jcb.200409058","article-title":"Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing","volume":"168","author":"Evans","year":"2005","journal-title":"J. Cell Biol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.cub.2005.02.029","article-title":"The Drosophila Homologue of the Hereditary Spastic Paraplegia Protein, Spastin, Severs and Disassembles Microtubules","volume":"15","author":"Vale","year":"2005","journal-title":"Curr. Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.4161\/cc.20849","article-title":"Human Fidgetin is a microtubule severing the enzyme and minus-end depolymerase that regulates mitosis","volume":"11","author":"Mukherjee","year":"2012","journal-title":"Cell Cycle"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.tcb.2020.10.004","article-title":"Cutting, Amplifying, and Aligning Microtubules with Severing Enzymes","volume":"31","author":"Kuo","year":"2020","journal-title":"Trends Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"4057","DOI":"10.1083\/jcb.201612104","article-title":"Microtubule-severing enzymes: From cellular functions to molecular mechanism","volume":"217","author":"McNally","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1038\/ncb2206","article-title":"Drosophila katanin is a microtubule depolymerase that regulates cortical-microtubule plus-end interactions and cell migration","volume":"13","author":"Zhang","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1093\/genetics\/126.3.593","article-title":"Mutations affecting the meiotic and mitotic divisions of the early Caenorhabditis elegans embryo","volume":"126","author":"Kemphues","year":"1990","journal-title":"Genetics"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1083\/jcb.145.2.305","article-title":"An Essential Role for Katanin in Severing Microtubules in the Neuron","volume":"145","author":"Ahmad","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1016\/j.neuron.2015.05.046","article-title":"Building the Neuronal Microtubule Cytoskeleton","volume":"87","author":"Kapitein","year":"2015","journal-title":"Neuron"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/cm.21286","article-title":"Stability properties of neuronal microtubules","volume":"73","author":"Baas","year":"2016","journal-title":"Cytoskeleton"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1091\/mbc.9.5.1195","article-title":"A Role for Katanin-mediated Axonemal Severing during Chlamydomonas Deflagellation","volume":"9","author":"Lohret","year":"1998","journal-title":"Mol. Biol. Cell"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"eaau1504","DOI":"10.1126\/science.aau1504","article-title":"Severing enzymes amplify microtubule arrays through lattice GTP-tubulin incorporation","volume":"361","author":"Vemu","year":"2018","journal-title":"Science"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1083\/jcb.200208058","article-title":"Cytoplasmic linker proteins promote microtubule rescue in vivo","volume":"159","author":"Komarova","year":"2002","journal-title":"J. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1038\/360674a0","article-title":"Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons","volume":"360","author":"Chen","year":"1992","journal-title":"Nature"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/369488a0","article-title":"Altered microtubule organization in small-calibre axons of mice lacking tau protein","volume":"369","author":"Harada","year":"1994","journal-title":"Nature"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.1523\/JNEUROSCI.5927-11.2012","article-title":"Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer\u2019s Disease","volume":"32","author":"Shahpasand","year":"2012","journal-title":"J. Neurosci."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1083\/jcb.201007081","article-title":"Template-free 13-protofilament microtubule\u2013MAP assembly visualized at 8 \u00c5 resolution","volume":"191","author":"Fourniol","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1083\/jcb.201808065","article-title":"MAP7 family proteins regulate kinesin-1 recruitment and activation","volume":"218","author":"Hooikaas","year":"2019","journal-title":"J. Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.cell.2010.07.012","article-title":"Insights into Antiparallel Microtubule Crosslinking by PRC1, a Conserved Nonmotor Microtubule Binding Protein","volume":"142","author":"Subramanian","year":"2010","journal-title":"Cell"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.cell.2010.06.033","article-title":"A Minimal Midzone Protein Module Controls Formation and Length of Antiparallel Microtubule Overlaps","volume":"142","author":"Bieling","year":"2010","journal-title":"Cell"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1700209","DOI":"10.1002\/bies.201700209","article-title":"Microtubule Inner Proteins: A Meshwork of Luminal Proteins Stabilizing the Doublet Microtubule","volume":"40","author":"Ichikawa","year":"2018","journal-title":"Bioessays"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"52760","DOI":"10.7554\/eLife.52760","article-title":"The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications","volume":"9","author":"Khalifa","year":"2020","journal-title":"Elife"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/j.cell.2019.09.030","article-title":"Structure of the Decorated Ciliary Doublet Microtubule","volume":"179","author":"Ma","year":"2019","journal-title":"Cell"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"a022608","DOI":"10.1101\/cshperspect.a022608","article-title":"Microtubules and Microtubule-Associated Proteins","volume":"10","author":"Goodson","year":"2018","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1038\/nnano.2014.334","article-title":"Molecular wear of microtubules propelled by surface-adhered kinesins","volume":"10","author":"Dumont","year":"2015","journal-title":"Nat. Nanotechnol."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1038\/s41563-020-00905-0","article-title":"Self-repair protects microtubules from destruction by molecular motors","volume":"20","author":"Triclin","year":"2021","journal-title":"Nat. Mater."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1083\/jcb.201406055","article-title":"The tubulin code: Molecular components, readout mechanisms, and functions","volume":"206","author":"Janke","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"a028159","DOI":"10.1101\/cshperspect.a028159","article-title":"Posttranslational Modifications of Tubulin and Cilia","volume":"9","author":"Wloga","year":"2016","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/B978-0-12-407699-0.00002-9","article-title":"A Hypothesis on the Origin and Evolution of Tubulin","volume":"302","year":"2013","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.mcn.2017.03.002","article-title":"Tubulins and brain development\u2014The origins of functional specification","volume":"84","author":"Breuss","year":"2017","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/0092-8674(80)90481-X","article-title":"Mutation in a testis-specific \u03b2-tubulin in Drosophila: Analysis of its effects on meiosis and map location of the gene","volume":"21","author":"Kemphues","year":"1980","journal-title":"Cell"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S0960-9822(01)00150-6","article-title":"Axoneme-specific \u03b2-tubulin specialization: A Conserved C-Terminal Motif Specifies the Central Pair","volume":"11","author":"Nielsen","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1242\/jcs.112.3.395","article-title":"MEC-12, an alpha-tubulin required for touch sensitivity in C. elegans","volume":"112","author":"Fukushige","year":"1999","journal-title":"J. Cell Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1101\/gad.3.6.870","article-title":"mec-7 is a beta-tubulin gene required for the production of 15-protofilament microtubules in Caenorhabditis elegans","volume":"3","author":"Savage","year":"1989","journal-title":"Genes Dev."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/S0960-9822(01)00153-1","article-title":"A lineage-restricted and divergent \u03b2-tubulin isoform is essential for the biogenesis, structure and function of blood platelets","volume":"11","author":"Schwer","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/s41580-020-0214-3","article-title":"The tubulin code and its role in controlling microtubule properties and functions","volume":"21","author":"Janke","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.tcb.2014.10.004","article-title":"Post-translational modifications of tubulin: Pathways to functional diversity of microtubules","volume":"25","author":"Song","year":"2014","journal-title":"Trends Cell Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1091\/mbc.e05-07-0621","article-title":"Microtubule Regulation in Mitosis: Tubulin Phosphorylation by the Cyclin-dependent Kinase Cdk1","volume":"17","author":"Peris","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.neuron.2016.03.027","article-title":"Phosphorylation of \u03b2-Tubulin by the Down Syndrome Kinase, Minibrain\/DYRK1a, Regulates Microtubule Dynamics and Dendrite Morphogenesis","volume":"90","author":"McKenney","year":"2016","journal-title":"Neuron"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/0014-5793(88)80658-6","article-title":"Identification of the phosphorylated \u03b2-tubulin isotype in differentiated neuroblastoma cells","volume":"230","author":"Zimmermann","year":"1988","journal-title":"FEBS Lett."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"4755","DOI":"10.1074\/jbc.271.9.4755","article-title":"Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates \u03b1-Tubulin on Tyrosine","volume":"271","author":"Peters","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"14797","DOI":"10.1016\/S0021-9258(18)66942-X","article-title":"Substrate specificities of tyrosine-specific protein kinases toward cytoskeletal proteins in vitro","volume":"261","author":"Akiyama","year":"1986","journal-title":"J. Biol. Chem."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1083\/jcb.111.5.1959","article-title":"Tubulin is phosphorylated at tyrosine by pp60c-src in nerve growth cone membranes","volume":"111","author":"Matten","year":"1990","journal-title":"J. Cell Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1016\/j.cell.2016.07.005","article-title":"Dual Chromatin and Cytoskeletal Remodeling by SETD2","volume":"166","author":"Park","year":"2016","journal-title":"Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"4748","DOI":"10.1074\/jbc.RA119.010951","article-title":"The microtubule-associated histone methyltransferase SET8, facilitated by transcription factor LSF, methylates \u03b1-tubulin","volume":"295","author":"Chin","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1091\/mbc.8.4.637","article-title":"Posttranslational modification of tubulin by palmitoylation: II. Identification of sites of palmitoylation","volume":"8","author":"Ozols","year":"1997","journal-title":"Mol. Biol. Cell"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.neuron.2013.01.036","article-title":"Transglutaminase and Polyamination of Tubulin: Posttranslational Modification for Stabilizing Axonal Microtubules","volume":"78","author":"Song","year":"2013","journal-title":"Neuron"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/0014-5793(77)80968-X","article-title":"Release of tyrosine from tyrosinated tubulin. Some common factors that affect this process and the assembly of tubulin","volume":"73","author":"Hallak","year":"1977","journal-title":"FEBS Lett."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1111\/j.1471-4159.1973.tb07578.x","article-title":"Incorporation of phenylalanine as a single unit into rat brain protein: Reciprocal inhibition by phenylalanine and tyrosine of their respective incorporations","volume":"21","author":"Barra","year":"1973","journal-title":"J. Neurochem."},{"key":"ref_122","first-page":"145","article-title":"Incorporation of l-Tyrosine, l-Phenylalanine and l-3,4-Dihydroxyphenylalanine as Single Units into Rat Brain Tubulin","volume":"59","author":"Arce","year":"1975","journal-title":"JBIC J. Biol. Inorg. Chem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1126\/science.7992051","article-title":"Polyglycylation of Tubulin: A Posttranslational Modification in Axonemal Microtubules","volume":"266","author":"Redeker","year":"1994","journal-title":"Science"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1242\/jcs.109.4.727","article-title":"Axonemal tubulin polyglycylation probed with two monoclonal antibodies: Widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility","volume":"109","author":"Bre","year":"1996","journal-title":"J. Cell Sci."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1126\/science.1967194","article-title":"Posttranslational Glutamylation of \u03b1-tubulin","volume":"247","author":"Rossier","year":"1990","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"4685","DOI":"10.1073\/pnas.88.11.4685","article-title":"Characterization of posttranslational modifications in neuron-specific class III beta-tubulin by mass spectrometry","volume":"88","author":"Hunt","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/0014-5793(92)81061-P","article-title":"Class II tubulin, the major brain \u03b2 tubulin isotype is polyglutamylated on glutamic acid residue 435","volume":"308","author":"Plessman","year":"1992","journal-title":"FEBS Lett."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"3316","DOI":"10.1523\/JNEUROSCI.23-08-03316.2003","article-title":"Parkin Binds to \u03b1\/\u03b2 Tubulin and Increases their Ubiquitination and Degradation","volume":"23","author":"Ren","year":"2003","journal-title":"J. Neurosci."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"jcs.229047","DOI":"10.1242\/jcs.229047","article-title":"Poly-ubiquitylation of \u03b1-tubulin at K304 is required for flagellar disassembly in Chlamydomonas","volume":"132","author":"Wang","year":"2019","journal-title":"J. Cell Sci."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1074\/mcp.M400149-MCP200","article-title":"A Universal Strategy for Proteomic Studies of SUMO and Other Ubiquitin-like Modifiers","volume":"4","author":"Russell","year":"2005","journal-title":"Mol. Cell. Proteom."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"2698","DOI":"10.1021\/bi00432a050","article-title":"Complete separation of tyrosinated, detyrosinated, and nontyrosinatable brain tubulin subpopulations using affinity chromatography","volume":"28","author":"Paturle","year":"1989","journal-title":"Biochemistry"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"10523","DOI":"10.1021\/bi00107a022","article-title":"Characterization of a major brain tubulin variant which cannot be tyrosinated","volume":"30","author":"Edde","year":"1991","journal-title":"Biochemistry"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"640","DOI":"10.1091\/mbc.E15-03-0137","article-title":"Evidence for new C-terminally truncated variants of \u03b1- and \u03b2-tubulins","volume":"27","author":"Aillaud","year":"2016","journal-title":"Mol. Biol. Cell"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1038\/s41467-019-09024-0","article-title":"Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation","volume":"10","author":"Hansen","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"16869","DOI":"10.1038\/srep16869","article-title":"New HDAC6-mediated deacetylation sites of tubulin in the mouse brain identified by quantitative mass spectrometry","volume":"5","author":"Liu","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"3292","DOI":"10.1021\/acs.jproteome.5b00308","article-title":"Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin","volume":"14","author":"Liu","year":"2015","journal-title":"J. Proteome Res."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.celrep.2012.07.006","article-title":"Proteomic Analysis of Lysine Acetylation Sites in Rat Tissues Reveals Organ Specificity and Subcellular Patterns","volume":"2","author":"Lundby","year":"2012","journal-title":"Cell Rep."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"ra48","DOI":"10.1126\/scisignal.2001902","article-title":"Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation","volume":"4","author":"Weinert","year":"2011","journal-title":"Sci. Signal."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1126\/science.1175371","article-title":"Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions","volume":"325","author":"Choudhary","year":"2009","journal-title":"Science"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1042\/BJ20131581","article-title":"Identification of protein succination as a novel modification of tubulin","volume":"462","author":"Piroli","year":"2014","journal-title":"Biochem. J."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1007\/s00726-010-0698-9","article-title":"O-GlcNAcylation of tubulin inhibits its polymerization","volume":"40","author":"Ji","year":"2010","journal-title":"Amino Acids"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.4161\/cc.6.17.4633","article-title":"The Tubulin Code","volume":"6","author":"Verhey","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_143","first-page":"119241","article-title":"Direct and indirect effects of tubulin post-translational modifications on microtubule stability: Insights and regulations","volume":"15","author":"Popp","year":"2022","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Res."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"7678","DOI":"10.1016\/S0021-9258(19)69014-9","article-title":"Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin","volume":"256","author":"Kumar","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"21517","DOI":"10.1073\/pnas.1013728107","article-title":"The major \u03b1-tubulin K40 acetyltransferase \u03b1TAT1 promotes rapid ciliogenesis and efficient mechanosensation","volume":"107","author":"Shida","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"8395","DOI":"10.1021\/bi9804131","article-title":"Tubulin Polyglutamylase: Partial Purification and Enzymatic Properties","volume":"37","author":"Regnard","year":"1998","journal-title":"Biochemistry"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1091\/mbc.4.6.615","article-title":"Reversible Polyglutamylation of Alpha- and Beta-Tubulin and Microtubule Dynamics in Mouse Brain Neurons","volume":"4","author":"Audebert","year":"1993","journal-title":"Mol. Biol. Cell"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1093\/emboj\/cdg115","article-title":"HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo","volume":"22","author":"Zhang","year":"2003","journal-title":"EMBO J."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1038\/nsmb.2148","article-title":"Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin","volume":"18","author":"Szyk","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1083\/jcb.201211017","article-title":"Structural basis of tubulin tyrosination by tubulin tyrosine ligase","volume":"200","author":"Prota","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s41048-020-00111-0","article-title":"The emerging role of tubulin posttranslational modifications in cilia and ciliopathies","volume":"6","author":"He","year":"2020","journal-title":"Biophys. Rep."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"2701","DOI":"10.1083\/jcb.201612050","article-title":"Tubulin glycylation controls primary cilia length","volume":"216","author":"Gadadhar","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1076","DOI":"10.1016\/j.cell.2009.05.020","article-title":"Evolutionary Divergence of Enzymatic Mechanisms for Posttranslational Polyglycylation","volume":"137","author":"Rogowski","year":"2009","journal-title":"Cell"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1016\/j.devcel.2009.04.008","article-title":"TTLL3 Is a Tubulin Glycine Ligase that Regulates the Assembly of Cilia","volume":"16","author":"Wloga","year":"2009","journal-title":"Dev. Cell"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1093\/brain\/awab200","article-title":"Neuronal SETD2 activity links microtubule methylation to an anxiety-like phenotype in mice","volume":"144","author":"Koenning","year":"2021","journal-title":"Brain"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"4113","DOI":"10.1038\/s41467-021-24376-2","article-title":"\u03b1-TubK40me3 is required for neuronal polarization and migration by promoting microtubule formation","volume":"12","author":"Xie","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.aai8764","article-title":"Microtubules acquire resistance from mechanical breakage through intralumenal acetylation","volume":"356","author":"Xu","year":"2017","journal-title":"Science"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"926914","DOI":"10.3389\/fcell.2022.926914","article-title":"Crosstalk between acetylation and the tyrosination\/detyrosination cycle of \u03b1-tubulin in Alzheimer\u2019s disease","volume":"10","author":"Parato","year":"2022","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.cell.2010.10.014","article-title":"A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration","volume":"143","author":"Rogowski","year":"2010","journal-title":"Cell"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1016\/j.cell.2018.05.018","article-title":"Tubulin Posttranslational Modifications and Emerging Links to Human Disease","volume":"173","author":"Magiera","year":"2018","journal-title":"Cell"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"17163","DOI":"10.1074\/jbc.R115.637447","article-title":"Writing and Reading the Tubulin Code","volume":"290","author":"Yu","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.cub.2009.12.058","article-title":"Tubulin Polyglutamylation Regulates Axonemal Motility by Modulating Activities of Inner-Arm Dyneins","volume":"20","author":"Kubo","year":"2010","journal-title":"Curr. Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.cub.2009.12.062","article-title":"Tubulin Glutamylation Regulates Ciliary Motility by Altering Inner Dynein Arm Activity","volume":"20","author":"Suryavanshi","year":"2010","journal-title":"Curr. Biol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1242\/jcs.111.3.313","article-title":"The axonemal microtubules of the Chlamydomonas flagellum differ in tubulin isoform content","volume":"111","author":"Johnson","year":"1998","journal-title":"J. Cell Sci."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1038\/nature09324","article-title":"MEC-17 is an \u03b1-tubulin acetyltransferase","volume":"467","author":"Akella","year":"2010","journal-title":"Nature"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"20334","DOI":"10.1074\/jbc.M113.464792","article-title":"Mice Lacking \u03b1-Tubulin Acetyltransferase 1 Are Viable but Display \u03b1-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion","volume":"288","author":"Kim","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1962","DOI":"10.1038\/ncomms2962","article-title":"\u03b1TAT1 is the major \u03b1-tubulin acetyltransferase in mice","volume":"4","author":"Kalebic","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1854","DOI":"10.1091\/mbc.e13-10-0609","article-title":"\u03b1-Tubulin K40 acetylation is required for contact inhibition of proliferation and cell\u2013substrate adhesion","volume":"25","author":"Aguilar","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"2927","DOI":"10.4161\/cc.5.24.3572","article-title":"Eukaryotic Domain of Unknown Function DUF738 Belongs to Gcn5-related N-acetyltransferase Superfamily","volume":"5","author":"Steczkiewicz","year":"2006","journal-title":"Cell Cycle"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"19655","DOI":"10.1073\/pnas.1209357109","article-title":"Structure of the \u03b1-tubulin acetyltransferase, \u03b1TAT1, and implications for tubulin-specific acetylation","volume":"109","author":"Friedmann","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"41569","DOI":"10.1074\/jbc.C112.421222","article-title":"Crystal Structures of Tubulin Acetyltransferase Reveal a Conserved Catalytic Core and the Plasticity of the Essential N Terminus","volume":"287","author":"Kormendi","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1707","DOI":"10.1038\/cr.2012.154","article-title":"Molecular basis of the acetyltransferase activity of MEC-17 towards \u03b1-tubulin","volume":"22","author":"Li","year":"2012","journal-title":"Cell Res."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"19649","DOI":"10.1073\/pnas.1209343109","article-title":"Atomic resolution structure of human \u03b1-tubulin acetyltransferase bound to acetyl-CoA","volume":"109","author":"Taschner","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.abb.2004.09.003","article-title":"Structure and functions of the GNAT superfamily of acetyltransferases","volume":"433","author":"Vetting","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1016\/j.cub.2021.12.012","article-title":"Acetylated \u03b1-tubulin K394 regulates microtubule stability to shape the growth of axon terminals","volume":"32","author":"Saunders","year":"2022","journal-title":"Curr. Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1091\/mbc.e10-03-0203","article-title":"A novel acetylation of \u03b2-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation","volume":"22","author":"Chu","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"2605","DOI":"10.1016\/j.jmb.2014.05.009","article-title":"Structural and Functional Characterization of the \u03b1-Tubulin Acetyltransferase MEC-17","volume":"426","author":"Davenport","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1111\/j.1365-2443.2008.01235.x","article-title":"N-acetyltransferase ARD1-NAT1 regulates neuronal dendritic development","volume":"13","author":"Ohkawa","year":"2008","journal-title":"Genes Cells"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/j.cell.2010.06.037","article-title":"Myc-Nick: A Cytoplasmic Cleavage Product of Myc that Promotes \u03b1-Tubulin Acetylation and Cell Differentiation","volume":"142","author":"Ngouenet","year":"2010","journal-title":"Cell"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.cell.2008.11.043","article-title":"Elongator Controls the Migration and Differentiation of Cortical Neurons through Acetylation of \u03b1-Tubulin","volume":"136","author":"Creppe","year":"2009","journal-title":"Cell"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.1016\/j.yexcr.2009.03.007","article-title":"NAT10, a nucleolar protein, localizes to the midbody and regulates cytokinesis and acetylation of microtubules","volume":"315","author":"Shen","year":"2009","journal-title":"Exp. Cell Res."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1016\/j.cub.2003.11.018","article-title":"Two Putative Acetyltransferases, San and Deco, Are Required for Establishing Sister Chromatid Cohesion in Drosophila","volume":"13","author":"Williams","year":"2003","journal-title":"Curr. Biol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1083\/jcb.200701043","article-title":"The acetyltransferase activity of San stabilizes the mitotic cohesin at the centromeres in a shugoshin-independent manner","volume":"177","author":"Hou","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1083\/jcb.129.5.1301","article-title":"Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila","volume":"129","author":"Gaertig","year":"1995","journal-title":"J. Cell Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"e00088-15","DOI":"10.1128\/mSphere.00088-15","article-title":"TgATAT-Mediated \u03b1-Tubulin Acetylation Is Required for Division of the Protozoan Parasite Toxoplasma gondii","volume":"1","author":"Varberg","year":"2016","journal-title":"Msphere"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1016\/j.ejcb.2012.07.001","article-title":"ATAT1\/MEC-17 acetyltransferase and HDAC6 deacetylase control a balance of acetylation of alpha-tubulin and cortactin and regulate MT1-MMP trafficking and breast tumor cell invasion","volume":"91","author":"Janke","year":"2012","journal-title":"Eur. J. Cell Biol."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1128\/MCB.01044-12","article-title":"Tubulin Acetyltransferase \u03b1TAT1 Destabilizes Microtubules Independently of Its Acetylation Activity","volume":"33","author":"Kalebic","year":"2013","journal-title":"Mol. Cell. Biol."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1126\/science.2646709","article-title":"Genetic Control of Differentiation of the Caenorhabditis elegans Touch Receptor Neurons","volume":"243","author":"Chalfie","year":"1989","journal-title":"Science"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nature00891","article-title":"Identification of genes expressed in C. elegans touch receptor neurons","volume":"418","author":"Zhang","year":"2002","journal-title":"Nature"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1016\/j.cub.2012.03.066","article-title":"Genetically Separable Functions of the MEC-17 Tubulin Acetyltransferase Affect Microtubule Organization","volume":"22","author":"Topalidou","year":"2012","journal-title":"Curr. Biol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1093\/abbs\/gmp070","article-title":"Cortactin is involved in transforming growth factor-\u03b21-induced epithelial-mesenchymal transition in AML-12 cells","volume":"41","author":"Zhang","year":"2009","journal-title":"Acta Biochim. Biophys. Sin."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nature12571","article-title":"\u03b1TAT1 catalyses microtubule acetylation at clathrin-coated pits","volume":"502","author":"Montagnac","year":"2013","journal-title":"Nature"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0092-8674(00)80961-7","article-title":"High-Resolution Model of the Microtubule","volume":"96","author":"Nogales","year":"1999","journal-title":"Cell"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Soppina, V., Herbstman, J.F., Skiniotis, G., and Verhey, K.J. (2012). Luminal Localization of \u03b1-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0048204"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.cell.2014.03.061","article-title":"Molecular Basis for Age-Dependent Microtubule Acetylation by Tubulin Acetyltransferase","volume":"157","author":"Szyk","year":"2014","journal-title":"Cell"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"E7176","DOI":"10.1073\/pnas.1605397113","article-title":"Mechanism of microtubule lumen entry for the \u03b1-tubulin acetyltransferase enzyme \u03b1TAT1","volume":"113","author":"Coombes","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"35624","DOI":"10.1038\/srep35624","article-title":"\u03b1TAT1 controls longitudinal spreading of acetylation marks from open microtubules extremities","volume":"6","author":"Ly","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1007\/s002490050161","article-title":"Diffusion inside microtubules","volume":"27","author":"Odde","year":"1998","journal-title":"Eur. Biophys. J."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1038\/nrm4084","article-title":"Control of microtubule organization and dynamics: Two ends in the limelight","volume":"16","author":"Akhmanova","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1083\/jcb.117.5.1031","article-title":"Lattice defects in microtubules: Protofilament numbers vary within individual microtubules","volume":"117","author":"Metoz","year":"1992","journal-title":"J. Cell Biol."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1038\/nmat4396","article-title":"Microtubules self-repair in response to mechanical stress","volume":"14","author":"Schaedel","year":"2015","journal-title":"Nat. Mater."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1091\/mbc.e13-07-0387","article-title":"Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure","volume":"25","author":"Howes","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"R1287","DOI":"10.1016\/j.cub.2017.10.044","article-title":"Causes and Consequences of Microtubule Acetylation","volume":"27","author":"Janke","year":"2017","journal-title":"Curr. Biol."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/417455a","article-title":"HDAC6 is a microtubule-associated deacetylase","volume":"417","author":"Hubbert","year":"2002","journal-title":"Nature"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1128\/MCB.01154-06","article-title":"Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally","volume":"28","author":"Zhang","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/S1097-2765(03)00038-8","article-title":"The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase","volume":"11","author":"North","year":"2003","journal-title":"Mol. Cell"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"13140","DOI":"10.1096\/fj.202001301RR","article-title":"Critical review of non-histone human substrates of metal-dependent lysine deacetylases","volume":"34","author":"Toro","year":"2020","journal-title":"FASEB J."},{"key":"ref_208","first-page":"146493","article-title":"Beyond Histone and Deacetylase: An Overview of Cytoplasmic Histone Deacetylases and Their Nonhistone Substrates","volume":"2011","author":"Yao","year":"2010","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1101\/gad.1412706","article-title":"SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis","volume":"20","author":"Vaquero","year":"2006","journal-title":"Genes Dev."},{"key":"ref_210","doi-asserted-by":"crossref","unstructured":"North, B.J., and Verdin, E. (2007). Interphase Nucleo-Cytoplasmic Shuttling and Localization of SIRT2 during Mitosis. PLoS ONE, 2.","DOI":"10.1371\/journal.pone.0000784"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"3173","DOI":"10.1128\/MCB.23.9.3173-3185.2003","article-title":"Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle","volume":"23","author":"Dryden","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.ccr.2011.09.004","article-title":"SIRT2 Maintains Genome Integrity and Suppresses Tumorigenesis through Regulating APC\/C Activity","volume":"20","author":"Kim","year":"2011","journal-title":"Cancer Cell"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"13546","DOI":"10.1073\/pnas.1301463110","article-title":"SIRT2 directs the replication stress response through CDK9 deacetylation","volume":"110","author":"Zhang","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1083\/jcb.200707126","article-title":"The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility","volume":"180","author":"Pandithage","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"de Oliveira, R.M., Vicente Miranda, H., Francelle, L., Pinho, R., Szeg\u00f6, \u00c9.M., Martinho, R., Munari, F., L\u00e1zaro, D.F., Moniot, S., and Guerreiro, P. (2017). The mechanism of sirtuin 2\u2013mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease. PLoS Biol., 15.","DOI":"10.1371\/journal.pbio.2000374"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/j.chembiol.2016.05.015","article-title":"SIRT2- and NRF2-Targeting Thiazole-Containing Compound with Therapeutic Activity in Huntington\u2019s Disease Models","volume":"23","author":"Quinti","year":"2016","journal-title":"Cell Chem. Biol."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.3233\/JAD-151135","article-title":"Sirtuin 2 Inhibition Improves Cognitive Performance and Acts on Amyloid-\u03b2 Protein Precursor Processing in Two Alzheimer\u2019s Disease Mouse Models","volume":"53","author":"Biella","year":"2016","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1021\/cb700160d","article-title":"Linking SIRT2 to Parkinson\u2019s Disease","volume":"2","author":"Garske","year":"2007","journal-title":"ACS Chem. Biol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"29168","DOI":"10.1074\/jbc.M112.371120","article-title":"Modulation of Histone Deacetylase 6 (HDAC6) Nuclear Import and Tubulin Deacetylase Activity through Acetylation","volume":"287","author":"Liu","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1111\/febs.12079","article-title":"Histone deacetylase 6 plays a role as a distinct regulator of diverse cellular processes","volume":"280","author":"Li","year":"2012","journal-title":"FEBS J."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.cellsig.2013.11.036","article-title":"HDAC6 mediates the acetylation of TRIM50","volume":"26","author":"Fusco","year":"2014","journal-title":"Cell. Signal."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/S0092-8674(03)00939-5","article-title":"The Deacetylase HDAC6 Regulates Aggresome Formation and Cell Viability in Response to Misfolded Protein Stress","volume":"115","author":"Kawaguchi","year":"2003","journal-title":"Cell"},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"5468","DOI":"10.1038\/sj.onc.1210614","article-title":"HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination","volume":"26","author":"Boyault","year":"2007","journal-title":"Oncogene"},{"key":"ref_224","doi-asserted-by":"crossref","unstructured":"Chen, S., Owens, G.C., Makarenkova, H., and Edelman, D.B. (2010). HDAC6 Regulates Mitochondrial Transport in Hippocampal Neurons. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0010848"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1186\/1750-1326-8-7","article-title":"HDAC6 as a target for neurodegenerative diseases: What makes it different from the other HDACs?","volume":"8","author":"Zwick","year":"2013","journal-title":"Mol. Neurodegener."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1021\/acsmedchemlett.9b00560","article-title":"Structural and in Vivo Characterization of Tubastatin A, a Widely Used Histone Deacetylase 6 Inhibitor","volume":"11","author":"Shen","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13045-018-0654-9","article-title":"Histone deacetylase 6 in cancer","volume":"11","author":"Li","year":"2018","journal-title":"J. Hematol. Oncol."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"8035","DOI":"10.1128\/MCB.21.23.8035-8044.2001","article-title":"Identification of Components of the Murine Histone Deacetylase 6 Complex: Link between Acetylation and Ubiquitination Signaling Pathways","volume":"21","author":"Verdel","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"2172","DOI":"10.1101\/gad.436407","article-title":"HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates","volume":"21","author":"Boyault","year":"2007","journal-title":"Genes Dev."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1083\/jcb.104.2.289","article-title":"Microtubules containing acetylated alpha-tubulin in mammalian cells in culture","volume":"104","author":"Piperno","year":"1987","journal-title":"J. Cell Biol."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"6820","DOI":"10.1093\/emboj\/cdf682","article-title":"In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation","volume":"21","author":"Matsuyama","year":"2002","journal-title":"EMBO J."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"555","DOI":"10.2174\/092986610791112620","article-title":"Histone Deacetylase 6 (HDAC6) Is an Independent Deacetylase for \u03b1-Tubulin","volume":"17","author":"Zhao","year":"2010","journal-title":"Protein Pept. Lett."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/nchembio.2140","article-title":"Structural insights into HDAC6 tubulin deacetylation and its selective inhibition","volume":"12","author":"Miyake","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"3531","DOI":"10.1242\/jcs.046813","article-title":"Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6","volume":"122","author":"Zilberman","year":"2009","journal-title":"J. Cell Sci."},{"key":"ref_235","doi-asserted-by":"crossref","unstructured":"Bobrowska, A., Donmez, G., Weiss, A., Guarente, L.P., and Bates, G.P. (2012). SIRT2 Ablation Has No Effect on Tubulin Acetylation in Brain, Cholesterol Biosynthesis or the Progression of Huntington\u2019s Disease Phenotypes In Vivo. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0034805"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"2972","DOI":"10.1242\/jcs.187518","article-title":"SIRT2 inactivation reveals a subset of hyperacetylated perinuclear microtubules inaccessible to HDAC6","volume":"129","author":"Skoge","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1242\/jcs.03431","article-title":"HDAC6 deacetylation of tubulin modulates dynamics of cellular adhesions","volume":"120","author":"Tran","year":"2007","journal-title":"J. Cell Sci."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"3435","DOI":"10.1091\/mbc.e06-01-0008","article-title":"Lymphocyte Chemotaxis Is Regulated by Histone Deacetylase 6, Independently of Its Deacetylase Activity","volume":"17","author":"Cabrero","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.molcel.2007.05.033","article-title":"HDAC6 Modulates Cell Motility by Altering the Acetylation Level of Cortactin","volume":"27","author":"Zhang","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1016\/j.cell.2007.04.035","article-title":"HEF1-Dependent Aurora A Activation Induces Disassembly of the Primary Cilium","volume":"129","author":"Pugacheva","year":"2007","journal-title":"Cell"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1038\/cr.2014.136","article-title":"CYLD mediates ciliogenesis in multiple organs by deubiquitinating Cep70 and inactivating HDAC6","volume":"24","author":"Yang","year":"2014","journal-title":"Cell Res."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"1644","DOI":"10.1093\/hmg\/ddt556","article-title":"SIRT2 regulates ciliogenesis and contributes to abnormal centrosome amplification caused by loss of polycystin-1","volume":"23","author":"Zhou","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/ncb3091","article-title":"Lineage specificity of primary cilia in the mouse embryo","volume":"17","author":"Bangs","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"12917","DOI":"10.1038\/srep12917","article-title":"Deacetylation of \u03b1-tubulin and cortactin is required for HDAC6 to trigger ciliary disassembly","volume":"5","author":"Ran","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"1787","DOI":"10.1007\/s00018-016-2148-7","article-title":"Mechanism of ciliary disassembly","volume":"73","author":"Liang","year":"2016","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"11816","DOI":"10.1074\/jbc.M113.507400","article-title":"Reactive Oxygen Species, AMP-activated Protein Kinase, and the Transcription Cofactor p300 Regulate \u03b1-Tubulin Acetyltransferase-1 (\u03b1TAT-1\/MEC-17)-dependent Microtubule Hyperacetylation during Cell Stress","volume":"289","author":"Mackeh","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.bbrc.2009.03.147","article-title":"Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity","volume":"383","author":"Han","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_248","first-page":"1","article-title":"ATP-citrate lyase promotes axonal transport across species","volume":"12","author":"Even","year":"2021","journal-title":"Nat. Commun."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1210\/er.2009-0026","article-title":"The Secret Life of NAD+: An Old Metabolite Controlling New Metabolic Signaling Pathways","volume":"31","author":"Houtkooper","year":"2010","journal-title":"Endocr. Rev."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.cmet.2015.05.023","article-title":"NAD+ Metabolism and the Control of Energy Homeostasis: A Balancing Act between Mitochondria and the Nucleus","volume":"22","author":"Menzies","year":"2015","journal-title":"Cell Metab."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/s41580-020-00313-x","article-title":"NAD+ metabolism and its roles in cellular processes during ageing","volume":"22","author":"Covarrubias","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.ceb.2015.02.003","article-title":"Acetyl-CoA and the regulation of metabolism: Mechanisms and consequences","volume":"33","author":"Shi","year":"2015","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1083\/jcb.101.6.2085","article-title":"Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms","volume":"101","author":"Piperno","year":"1985","journal-title":"J. Cell Biol."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1073\/pnas.84.16.5720","article-title":"Identification of an acetylation site of Chlamydomonas alpha-tubulin","volume":"84","author":"LeDizet","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1016\/j.cell.2014.05.021","article-title":"A Slow Dance for Microtubule Acetylation","volume":"157","author":"Kull","year":"2014","journal-title":"Cell"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1083\/jcb.103.2.571","article-title":"The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules","volume":"103","author":"Maruta","year":"1986","journal-title":"J. Cell Biol."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/421230a","article-title":"Tubulin acetylation and cell motility","volume":"421","author":"Palazzo","year":"2003","journal-title":"Nature"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1242\/jcs.92.1.57","article-title":"Microtubules are acetylated in domains that turn over slowly","volume":"92","author":"Webster","year":"1989","journal-title":"J. Cell Sci."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1073\/pnas.0430973100","article-title":"Domain-selective small-molecule inhibitor of histone deacetylase 6 (HDAC6)-mediated tubulin deacetylation","volume":"100","author":"Haggarty","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cub.2012.05.012","article-title":"Posttranslational Acetylation of \u03b1-Tubulin Constrains Protofilament Number in Native Microtubules","volume":"22","author":"Cueva","year":"2012","journal-title":"Curr. Biol."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1007\/s002490050159","article-title":"Limited flexibility of the inter-protofilament bonds in microtubules assembled from pure tubulin","volume":"27","author":"Flyvbjerg","year":"1998","journal-title":"Eur. Biophys. J."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"3803","DOI":"10.1016\/j.jbiomech.2016.10.008","article-title":"Role of the inter-protofilament sliding in the bending of protein microtubules","volume":"49","author":"Wang","year":"2016","journal-title":"J. Biomech."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"10366","DOI":"10.1073\/pnas.1900441116","article-title":"Effects of \u03b1-tubulin acetylation on microtubule structure and stability","volume":"116","author":"Zhang","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_264","first-page":"391","article-title":"Tubulin acetylation protects long-lived microtubules against mechanical ageing","volume":"19","author":"Portran","year":"2017","journal-title":"Nature"},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.celrep.2013.12.004","article-title":"Loss of MEC-17 Leads to Microtubule Instability and Axonal Degeneration","volume":"6","author":"Neumann","year":"2014","journal-title":"Cell Rep."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/dneu.22774","article-title":"Tubulin post-translational modifications control neuronal development and functions","volume":"81","author":"Moutin","year":"2020","journal-title":"Dev. Neurobiol."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1242\/dev.097774","article-title":"Microtubule-severing protein Katanin regulates neuromuscular junction development and dendritic elaboration in Drosophila","volume":"141","author":"Mao","year":"2014","journal-title":"Development"},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"7215","DOI":"10.1523\/JNEUROSCI.0048-10.2010","article-title":"Acetylation of Microtubules Influences Their Sensitivity to Severing by Katanin in Neurons and Fibroblasts","volume":"30","author":"Sudo","year":"2010","journal-title":"J. Neurosci."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1016\/j.celrep.2015.08.017","article-title":"Vertebrate Fidgetin Restrains Axonal Growth by Severing Labile Domains of Microtubules","volume":"12","author":"Leo","year":"2015","journal-title":"Cell Rep."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1007\/s00795-018-0195-x","article-title":"Dynamic localization of \u03b1-tubulin acetyltransferase ATAT1 through the cell cycle in human fibroblastic KD cells","volume":"51","author":"Nakakura","year":"2018","journal-title":"Med. Mol. Morphol."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/bi00323a034","article-title":"Chlamydomonas. alpha.-tubulin is posttranslationally modified by acetylation on the.epsilon.-amino group of a lysine","volume":"24","author":"Rosenbaum","year":"1985","journal-title":"Biochemistry"},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/s00795-015-0132-1","article-title":"Intracellular localization of \u03b1-tubulin acetyltransferase ATAT1 in rat ciliated cells","volume":"49","author":"Nakakura","year":"2015","journal-title":"Med. Mol. Morphol."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1007\/s00795-014-0076-x","article-title":"The elongation of primary cilia via the acetylation of \u03b1-tubulin by the treatment with lithium chloride in human fibroblast KD cells","volume":"48","author":"Nakakura","year":"2014","journal-title":"Med. Mol. Morphol."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"4372","DOI":"10.1172\/JCI57552","article-title":"Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered in Huntington disease","volume":"121","author":"Keryer","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1016\/j.devcel.2008.11.001","article-title":"A BBSome Subunit Links Ciliogenesis, Microtubule Stability, and Acetylation","volume":"15","author":"Loktev","year":"2008","journal-title":"Dev. Cell"},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1002\/cm.970250205","article-title":"High level expression of nonacetylatable ?-tubulin inChlamydomonas reinhardtii","volume":"25","author":"Kozminski","year":"1993","journal-title":"Cell Motil. Cytoskelet."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"2872","DOI":"10.1016\/j.bpj.2014.10.061","article-title":"The Motility of Axonemal Dynein Is Regulated by the Tubulin Code","volume":"107","author":"Alper","year":"2014","journal-title":"Biophys. J."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1016\/j.cub.2006.09.014","article-title":"Microtubule Acetylation Promotes Kinesin-1 Binding and Transport","volume":"16","author":"Reed","year":"2006","journal-title":"Curr. Biol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1016\/j.bpj.2014.05.008","article-title":"Effects of \u03b1-Tubulin K40 Acetylation and Detyrosination on Kinesin-1 Motility in a Purified System","volume":"106","author":"Kaul","year":"2014","journal-title":"Biophys. J."},{"key":"ref_280","doi-asserted-by":"crossref","unstructured":"Walter, W.J., Ber\u00e1nek, V., Fischermeier, E., and Diez, S. (2012). Tubulin Acetylation Alone Does Not Affect Kinesin-1 Velocity and Run Length In Vitro. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0042218"},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Sullenberger, C., Vasquez-Limeta, A., Kong, D., and Loncarek, J. (2020). With Age Comes Maturity: Biochemical and Structural Transformation of a Human Centriole in the Making. Cells, 9.","DOI":"10.3390\/cells9061429"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.semcdb.2021.12.001","article-title":"The centriolar tubulin code","volume":"137","author":"Guichard","year":"2023","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1111\/jmi.12841","article-title":"Expansion microscopy for the analysis of centrioles and cilia","volume":"276","author":"Sahabandu","year":"2019","journal-title":"J. Microsc."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s00795-020-00260-8","article-title":"Role of tubulin acetylation in cellular functions and diseases","volume":"53","author":"Hagiwara","year":"2020","journal-title":"Med. Mol. Morphol."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1523\/JNEUROSCI.13-02-00856.1993","article-title":"Regional differences in microtubule dynamics in the axon","volume":"13","author":"Ahmad","year":"1993","journal-title":"J. Neurosci."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1083\/jcb.104.6.1569","article-title":"Posttranslational modifications of alpha-tubulin: Acetylated and detyrosinated forms in axons of rat cerebellum","volume":"104","author":"Burgoyne","year":"1987","journal-title":"J. Cell Biol."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1242\/jcs.104.2.339","article-title":"Composite microtubules of the axon: Quantitative analysis of tyrosinated and acetylated tubulin along individual axonal microtubules","volume":"104","author":"Brown","year":"1993","journal-title":"J. Cell Sci."},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"e20813","DOI":"10.7554\/eLife.20813","article-title":"Acetylated tubulin is essential for touch sensation in mice","volume":"5","author":"Morley","year":"2016","journal-title":"Elife"},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1016\/j.cub.2009.06.036","article-title":"The Multipurpose 15-Protofilament Microtubules in C. elegans Have Specific Roles in Mechanosensation","volume":"19","author":"Bounoutas","year":"2009","journal-title":"Curr. Biol."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1016\/j.celrep.2018.09.075","article-title":"Microtubule Acetylation Is Required for Mechanosensation in Drosophila","volume":"25","author":"Yan","year":"2018","journal-title":"Cell Rep."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"1264","DOI":"10.1016\/j.neuron.2017.11.018","article-title":"Differentiation between Oppositely Oriented Microtubules Controls Polarized Neuronal Transport","volume":"96","author":"Tas","year":"2017","journal-title":"Neuron"},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/j.ejcb.2014.07.006","article-title":"Microtubule acetylation regulates dynamics of KIF1C-powered vesicles and contact of microtubule plus ends with podosomes","volume":"93","author":"Bhuwania","year":"2014","journal-title":"Eur. J. Cell Biol."},{"key":"ref_293","doi-asserted-by":"crossref","unstructured":"Cai, D., McEwen, D.P., Martens, J.R., Meyhofer, E., and Verhey, K.J. (2009). Single Molecule Imaging Reveals Differences in Microtubule Track Selection Between Kinesin Motors. PLOS Biol., 7.","DOI":"10.1371\/journal.pbio.1000216"},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"3571","DOI":"10.1523\/JNEUROSCI.0037-07.2007","article-title":"Histone Deacetylase 6 Inhibition Compensates for the Transport Deficit in Huntington\u2019s Disease by Increasing Tubulin Acetylation","volume":"27","author":"Dompierre","year":"2007","journal-title":"J. Neurosci."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"5245","DOI":"10.1038\/ncomms6245","article-title":"Increasing microtubule acetylation rescues axonal transport and locomotor deficits caused by LRRK2 Roc-COR domain mutations","volume":"5","author":"Godena","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1083\/jcb.200911024","article-title":"ER sliding dynamics and ER-mitochondrial contacts occur on acetylated microtubules","volume":"190","author":"Friedman","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1038\/ni.2550","article-title":"Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome","volume":"14","author":"Misawa","year":"2013","journal-title":"Nat. Immunol."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"eaax2705","DOI":"10.1126\/sciadv.aax2705","article-title":"ATAT1-enriched vesicles promote microtubule acetylation via axonal transport","volume":"5","author":"Even","year":"2019","journal-title":"Sci. Adv."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1042\/BCJ20160172","article-title":"The growing landscape of tubulin acetylation: Lysine 40 and many more","volume":"473","author":"Sadoul","year":"2016","journal-title":"Biochem. J."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"6353","DOI":"10.1074\/jbc.RA118.005765","article-title":"Polyglutamylation of tubulin\u2019s C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A","volume":"294","author":"Lessard","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"3119","DOI":"10.1091\/mbc.e14-01-0022","article-title":"Regulation of microtubule-based transport by MAP4","volume":"25","author":"Semenova","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"e36374","DOI":"10.7554\/eLife.36374","article-title":"MAP7 regulates axon morphogenesis by recruiting kinesin-1 to microtubules and modulating organelle transport","volume":"7","author":"Tymanskyj","year":"2018","journal-title":"Elife"},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1038\/s41467-018-03909-2","article-title":"Competition between microtubule-associated proteins directs motor transport","volume":"9","author":"Monroy","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_304","first-page":"1086","article-title":"Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes","volume":"21","author":"Siahaan","year":"2019","journal-title":"Nature"},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1242\/jcs.103.4.953","article-title":"Increased microtubule stability and alpha tubulin acetylation in cells transfected with microtubule-associated proteins MAP1B, MAP2 or tau","volume":"103","author":"Takemura","year":"1992","journal-title":"J. Cell Sci."},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1242\/jcs.102.2.227","article-title":"Expression of tau protein in non-neuronal cells: Microtubule binding and stabilization","volume":"102","author":"Lee","year":"1992","journal-title":"J. Cell Sci."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1023\/A:1007587315630","article-title":"Differential Association of Tau With Subsets of Microtubules Containing Posttranslationally-Modified Tubulin Variants in Neuroblastoma Cells","volume":"25","author":"Saragoni","year":"2000","journal-title":"Neurochem. Res."},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1111\/j.1471-4159.2009.06102.x","article-title":"Tau\u2014An inhibitor of deacetylase HDAC6 function","volume":"109","author":"Perez","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_309","first-page":"1245","article-title":"Increased acetylation of microtubules rescues human tau-induced microtubule defects and neuromuscular junction abnormalities in Drosophila","volume":"10","author":"Mao","year":"2017","journal-title":"Dis. Model. Mech."},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"2008","DOI":"10.1016\/j.bbadis.2018.11.014","article-title":"Acetylation as a major determinant to microtubule-dependent autophagy: Relevance to Alzheimer\u2019s and Parkinson disease pathology","volume":"1865","author":"Esteves","year":"2018","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1126\/science.aaa5175","article-title":"Microtubule detyrosination guides chromosomes during mitosis","volume":"348","author":"Barisic","year":"2015","journal-title":"Science"},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/cm.970140210","article-title":"Acetylated ?-tubulin in spermatogenic cells of the crane flyNephrotoma suturalis: Kinetochore microtubules are selectively acetylated","volume":"14","author":"Wilson","year":"1989","journal-title":"Cell Motil. Cytoskelet."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.semcdb.2021.11.014","article-title":"Tubulin post-translational modifications in meiosis","volume":"137","author":"Akera","year":"2023","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/0012-1606(88)90415-0","article-title":"Acetylated \u03b1-tubulin in microtubules during mouse fertilization and early development","volume":"130","author":"Schatten","year":"1988","journal-title":"Dev. Biol."},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1006\/cbir.1995.1006","article-title":"Acetylation of \u03b1-tubilin in different bovine cell types: Implications for microtubule dynamics in interphase and mitosis","volume":"19","author":"Wolf","year":"1995","journal-title":"Cell Biol. Int."},{"key":"ref_316","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0012-1606(89)90134-6","article-title":"The appearance of acetylated \u03b1-tubulin during early development and cellular differentiation in Xenopus","volume":"136","author":"Chu","year":"1989","journal-title":"Dev. Biol."},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.4161\/cc.6.9.4219","article-title":"The Molecular Biology of Mammalian SIRT Proteins: SIRT2 Functions on Cell Cycle Regulation","volume":"6","author":"Inoue","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"4369","DOI":"10.1242\/jcs.127209","article-title":"Furry promotes acetylation of microtubules in the mitotic spindle by inhibition of SIRT2 tubulin deacetylase","volume":"126","author":"Nagai","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_319","first-page":"131","article-title":"CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin","volume":"29","author":"Masoumi","year":"2009","journal-title":"EMBO J."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"4605","DOI":"10.1182\/blood-2007-10-118844","article-title":"Visualization of microtubule growth in living platelets reveals a dynamic marginal band with multiple microtubules","volume":"111","author":"Richardson","year":"2008","journal-title":"Blood"},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1182\/blood-2012-05-428011","article-title":"HDAC6 controls the kinetics of platelet activation","volume":"120","author":"Sadoul","year":"2012","journal-title":"Blood"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1083\/jcb.201403039","article-title":"Paxillin inhibits HDAC6 to regulate microtubule acetylation, Golgi structure, and polarized migration","volume":"206","author":"Deakin","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"5396","DOI":"10.1074\/jbc.M115.713123","article-title":"Loss of \u03b1-Tubulin Acetylation Is Associated with TGF-\u03b2-induced Epithelial-Mesenchymal Transition","volume":"291","author":"Gu","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1158\/0008-5472.CAN-13-3563","article-title":"\u03b1-Tubulin Acetylation Elevated in Metastatic and Basal-like Breast Cancer Cells Promotes Microtentacle Formation, Adhesion, and Invasive Migration","volume":"75","author":"Boggs","year":"2015","journal-title":"Cancer Res."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"jcs.225805","DOI":"10.1242\/jcs.225805","article-title":"Microtubule acetylation but not detyrosination promotes focal adhesion dynamics and astrocyte migration","volume":"132","author":"Bance","year":"2019","journal-title":"J. Cell Sci."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"109556","DOI":"10.1016\/j.celrep.2021.109556","article-title":"Tubulin acetylation promotes penetrative capacity of cells undergoing radial intercalation","volume":"36","author":"Collins","year":"2021","journal-title":"Cell Rep."},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/s41563-021-01108-x","article-title":"Microtubules tune mechanosensitive cell responses","volume":"21","author":"Seetharaman","year":"2021","journal-title":"Nat. Mater."},{"key":"ref_328","first-page":"2228","article-title":"The role of protein acetylation in carcinogenesis and targeted drug discovery","volume":"13","author":"Yang","year":"2022","journal-title":"Front. Endocrinol."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.1523\/JNEUROSCI.07-06-01833.1987","article-title":"Acetylation of alpha-tubulin in cultured neurons and the induction of alpha-tubulin acetylation in PC12 cells by treatment with nerve growth factor","volume":"7","author":"Black","year":"1987","journal-title":"J. Neurosci."},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"101511","DOI":"10.1016\/j.isci.2020.101511","article-title":"The Mechanism of Tubulin Assembly into Microtubules: Insights from Structural Studies","volume":"23","author":"Knossow","year":"2020","journal-title":"iScience"},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"24184","DOI":"10.1074\/jbc.M109.091553","article-title":"Starvation-induced Hyperacetylation of Tubulin Is Required for the Stimulation of Autophagy by Nutrient Deprivation","volume":"285","author":"Geeraert","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1186\/1471-2121-11-89","article-title":"Acetylated microtubules are required for fusion of autophagosomes with lysosomes","volume":"11","author":"Xie","year":"2010","journal-title":"BMC Cell Biol."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1006\/taap.1996.0243","article-title":"Nickel (Ni2+) Enhancement of \u03b1-Tubulin Acetylation in Cultured 3T3 Cells","volume":"140","author":"Li","year":"1996","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.cellsig.2008.12.004","article-title":"Tubulin acetylation favors Hsp90 recruitment to microtubules and stimulates the signaling function of the Hsp90 clients Akt\/PKB and p53","volume":"21","author":"Giustiniani","year":"2009","journal-title":"Cell. Signal."},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1165\/rcmb.2012-0161OC","article-title":"Oxidative Stress Contributes to Lung Injury and Barrier Dysfunction via Microtubule Destabilization","volume":"47","author":"Kratzer","year":"2012","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1126\/science.1200094","article-title":"AMPK Is a Direct Adenylate Charge-Regulated Protein Kinase","volume":"332","author":"Oakhill","year":"2011","journal-title":"Science"},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"25154","DOI":"10.1074\/jbc.M116.742247","article-title":"Activation of AMP-activated Protein Kinase by Metformin Induces Protein Acetylation in Prostate and Ovarian Cancer Cells","volume":"291","author":"Galdieri","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_338","doi-asserted-by":"crossref","unstructured":"Vancura, A., Nagar, S., Kaur, P., Bu, P., Bhagwat, M., and Vancurova, I. (2018). Reciprocal Regulation of AMPK\/SNF1 and Protein Acetylation. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19113314"},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"e47866","DOI":"10.7554\/eLife.47866","article-title":"Elevating acetyl-CoA levels reduces aspects of brain aging","volume":"8","author":"Currais","year":"2019","journal-title":"Elife"},{"key":"ref_340","doi-asserted-by":"crossref","unstructured":"Tarasiuk, O., Miceli, M., Di Domizio, A., and Nicolini, G. (2022). AMPK and Diseases: State of the Art Regulation by AMPK-Targeting Molecules. Biology, 11.","DOI":"10.3390\/biology11071041"},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"33154","DOI":"10.1074\/jbc.M110.143685","article-title":"Exposure to Hydrogen Peroxide Induces Oxidation and Activation of AMP-activated Protein Kinase*","volume":"285","author":"Zmijewski","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/s11010-013-1568-z","article-title":"TAK1 activates AMPK-dependent cell death pathway in hydrogen peroxide-treated cardiomyocytes, inhibited by heat shock protein-70","volume":"377","author":"Chen","year":"2013","journal-title":"Mol. Cell. Biochem."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"17208","DOI":"10.1074\/jbc.RA118.002579","article-title":"Mitochondria-derived ROS activate AMP-activated protein kinase (AMPK) indirectly","volume":"293","author":"Hinchy","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.arr.2011.12.005","article-title":"AMP-activated protein kinase (AMPK) controls the aging process via an integrated signaling network","volume":"11","author":"Salminen","year":"2012","journal-title":"Ageing Res. Rev."},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"e202202100","DOI":"10.1083\/jcb.202202100","article-title":"Non-catalytic allostery in \u03b1-TAT1 by a phospho-switch drives dynamic microtubule acetylation","volume":"221","author":"Roy","year":"2022","journal-title":"J. Cell Biol."},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-018-04121-y","article-title":"TAK1 activation of alpha-TAT1 and microtubule hyperacetylation control AKT signaling and cell growth","volume":"9","author":"Shah","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_347","first-page":"5389","article-title":"Analysis with Specific Polyclonal Antiserum Indicates That the E1A-Associated 300-KDa Product Is a Stable Nuclear Phosphoprotein That Undergoes Cell Cycle Phase-Specific Modification","volume":"11","author":"Yaciuk","year":"1991","journal-title":"Mol. Cell. Biol."},{"key":"ref_348","doi-asserted-by":"crossref","first-page":"38341","DOI":"10.1074\/jbc.C100316200","article-title":"Regulation of Transcription by AMP-activated Protein Kinase: Phosphorylation of P300 Blocks Its Interaction with Nuclear Receptors","volume":"276","author":"Yang","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_349","doi-asserted-by":"crossref","first-page":"2897","DOI":"10.1161\/ATVBAHA.111.237453","article-title":"AMP-Activated Protein Kinase Suppresses Endothelial Cell Inflammation Through Phosphorylation of Transcriptional Coactivator p300","volume":"31","author":"Zhang","year":"2011","journal-title":"Arter. Thromb. Vasc. Biol."},{"key":"ref_350","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1177\/1535370219868960","article-title":"Cardiac microtubules in health and heart disease","volume":"244","author":"Chen","year":"2019","journal-title":"Exp. Biol. Med."},{"key":"ref_351","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1242\/jcs.115626","article-title":"Autophagy and microtubules\u2014New story, old players","volume":"126","author":"Mackeh","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.cell.2017.02.004","article-title":"mTOR Signaling in Growth, Metabolism, and Disease","volume":"168","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"ref_353","doi-asserted-by":"crossref","unstructured":"Chun, Y., and Kim, J. (2018). Autophagy: An Essential Degradation Program for Cellular Homeostasis and Life. Cells, 7.","DOI":"10.3390\/cells7120278"},{"key":"ref_354","doi-asserted-by":"crossref","unstructured":"Ha\u0107, A., Pierzynowska, K., and Herman-Antosiewicz, A. (2021). S6K1 Is Indispensible for Stress-Induced Microtubule Acetylation and Autophagic Flux. Cells, 10.","DOI":"10.3390\/cells10040929"},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"964","DOI":"10.1097\/00005072-199609000-00003","article-title":"Reduction of Acetylated \u03b1-Tubulin Immunoreactivity in Neurofibrillary Tangle-bearing Neurons in Alzheimer\u02bcs Disease","volume":"55","author":"Hempen","year":"1996","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"ref_356","doi-asserted-by":"crossref","first-page":"4021","DOI":"10.1007\/s12035-016-9951-x","article-title":"Mitochondrial Metabolism Power SIRT2-Dependent Deficient Traffic Causing Alzheimer\u2019s-Disease Related Pathology","volume":"54","author":"Silva","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"ref_357","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1038\/nm.2396","article-title":"HDAC6 inhibitors reverse axonal loss in a mouse model of mutant HSPB1\u2013induced Charcot-Marie-Tooth disease","volume":"17","author":"Krishnan","year":"2011","journal-title":"Nat. Med."},{"key":"ref_358","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/s13311-016-0501-z","article-title":"Development of Improved HDAC6 Inhibitors as Pharmacological Therapy for Axonal Charcot\u2013Marie\u2013Tooth Disease","volume":"14","author":"Benoy","year":"2017","journal-title":"Neurotherapeutics"},{"key":"ref_359","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1021\/acschemneuro.9b00338","article-title":"Novel HDAC6 Inhibitors Increase Tubulin Acetylation and Rescue Axonal Transport of Mitochondria in a Model of Charcot\u2013Marie\u2013Tooth Type 2F","volume":"11","author":"Adalbert","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"113281","DOI":"10.1016\/j.expneurol.2020.113281","article-title":"HDAC6 inhibition promotes \u03b1-tubulin acetylation and ameliorates CMT2A peripheral neuropathy in mice","volume":"328","author":"Picci","year":"2020","journal-title":"Exp. Neurol."},{"key":"ref_361","doi-asserted-by":"crossref","first-page":"1783","DOI":"10.1093\/hmg\/ddt028","article-title":"Hdac6 deletion delays disease progression in the SOD1G93A mouse model of ALS","volume":"22","author":"Taes","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1002\/emmm.201201923","article-title":"Reducing HDAC6 ameliorates cognitive deficits in a mouse model for Alzheimer\u2019s disease","volume":"5","author":"Govindarajan","year":"2012","journal-title":"EMBO Mol. Med."},{"key":"ref_363","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.3233\/JAD-140066","article-title":"Tubastatin A\/ACY-1215 Improves Cognition in Alzheimer\u2019s Disease Transgenic Mice","volume":"41","author":"Zhang","year":"2014","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_364","doi-asserted-by":"crossref","first-page":"135900","DOI":"10.1016\/j.neulet.2021.135900","article-title":"Microtubule acetylation: A reading key to neural physiology and degeneration","volume":"755","author":"Cappelletti","year":"2021","journal-title":"Neurosci. Lett."},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"\u03b1-Synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"key":"ref_366","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1097\/WCO.0b013e3283484b87","article-title":"Genetics of Parkinson\u2019s disease and essential tremor","volume":"24","author":"Zimprich","year":"2011","journal-title":"Curr. Opin. Neurol."},{"key":"ref_367","doi-asserted-by":"crossref","first-page":"435","DOI":"10.3233\/JAD-2004-6412","article-title":"Demonstration of a role for \u03b1-synuclein as a functional microtubule-associated protein","volume":"6","author":"Alim","year":"2004","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"ref_368","doi-asserted-by":"crossref","first-page":"33289","DOI":"10.1038\/srep33289","article-title":"\u03b1-Synuclein is a Novel Microtubule Dynamase","volume":"6","author":"Cartelli","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_369","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1126\/science.1143780","article-title":"Sirtuin 2 Inhibitors Rescue \u03b1-Synuclein-Mediated Toxicity in Models of Parkinson\u2019s Disease","volume":"317","author":"Outeiro","year":"2007","journal-title":"Science"},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1042\/BST20180462","article-title":"LRRK2 links genetic and sporadic Parkinson\u2019s disease","volume":"47","author":"Kluss","year":"2019","journal-title":"Biochem. Soc. Trans."},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1038\/ng.487","article-title":"Genome-wide association study reveals genetic risk underlying Parkinson\u2019s disease","volume":"41","author":"Schulte","year":"2009","journal-title":"Nat. Genet."},{"key":"ref_372","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1038\/s41594-022-00863-y","article-title":"Structural basis for Parkinson\u2019s disease-linked LRRK2\u2032s binding to microtubules","volume":"29","author":"Snead","year":"2022","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_373","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1074\/jbc.M113.507913","article-title":"A Direct Interaction between Leucine-rich Repeat Kinase 2 and Specific \u03b2-Tubulin Isoforms Regulates Tubulin Acetylation","volume":"289","author":"Law","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_374","doi-asserted-by":"crossref","first-page":"2494","DOI":"10.1002\/mds.28755","article-title":"Structural Biology of LRRK2 and its Interaction with Microtubules","volume":"36","author":"Leschziner","year":"2021","journal-title":"Mov. Disord."},{"key":"ref_375","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/s41586-020-2673-2","article-title":"Structure of LRRK2 in Parkinson\u2019s disease and model for microtubule interaction","volume":"588","author":"Deniston","year":"2020","journal-title":"Nature"},{"key":"ref_376","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.freeradbiomed.2015.02.028","article-title":"Molecular mechanisms linking amyloid \u03b2 toxicity and Tau hyperphosphorylation in Alzheimer\u05f3s disease","volume":"83","author":"Lloret","year":"2015","journal-title":"Free. Radic. Biol. Med."},{"key":"ref_377","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1111\/j.1471-4159.2008.05564.x","article-title":"Histone deacetylase 6 interacts with the microtubule-associated protein tau","volume":"106","author":"Ding","year":"2008","journal-title":"J. Neurochem."},{"key":"ref_378","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1186\/alzrt241","article-title":"Histone deacetylase 6 inhibition improves memory and reduces total tau levels in a mouse model of tau deposition","volume":"6","author":"Selenica","year":"2014","journal-title":"Alzheimer\u2019s Res. Ther."},{"key":"ref_379","doi-asserted-by":"crossref","first-page":"2169","DOI":"10.1016\/j.celrep.2017.07.082","article-title":"The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology","volume":"20","author":"Tseng","year":"2017","journal-title":"Cell Rep."},{"key":"ref_380","doi-asserted-by":"crossref","first-page":"15423","DOI":"10.1038\/s41598-021-94923-w","article-title":"A novel orally active HDAC6 inhibitor T-518 shows a therapeutic potential for Alzheimer\u2019s disease and tauopathy in mice","volume":"11","author":"Onishi","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_381","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1126\/science.1152993","article-title":"Differential Regulation of Dynein and Kinesin Motor Proteins by Tau","volume":"319","author":"Dixit","year":"2008","journal-title":"Science"},{"key":"ref_382","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1038\/ncomms1255","article-title":"The acetylation of tau inhibits its function and promotes pathological tau aggregation","volume":"2","author":"Cohen","year":"2011","journal-title":"Nat. Commun."},{"key":"ref_383","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40035-015-0030-4","article-title":"Posttranslational modifications of \u03b1-tubulin in alzheimer disease","volume":"4","author":"Zhang","year":"2015","journal-title":"Transl. Neurodegener."},{"key":"ref_384","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1007\/s12105-013-0476-6","article-title":"Acetylated Tubulin (AT) as a Prognostic Marker in Squamous Cell Carcinoma of the Head and Neck","volume":"8","author":"Saba","year":"2013","journal-title":"Head Neck Pathol."},{"key":"ref_385","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1158\/0008-5472.CAN-08-1290","article-title":"Pancreatic Cancer and Precursor Pancreatic Intraepithelial Neoplasia Lesions Are Devoid of Primary Cilia","volume":"69","author":"Seeley","year":"2009","journal-title":"Cancer Res"},{"key":"ref_386","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1186\/1476-4598-13-230","article-title":"Histone deacetylase inhibition synergistically enhances pemetrexed cytotoxicity through induction of apoptosis and autophagy in non-small cell lung cancer","volume":"13","author":"Desideri","year":"2014","journal-title":"Mol. Cancer"},{"key":"ref_387","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.ejcb.2010.09.004","article-title":"HDAC6 is required for invadopodia activity and invasion by breast tumor cells","volume":"90","author":"Rey","year":"2011","journal-title":"Eur. J. Cell Biol."},{"key":"ref_388","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-35392-6","article-title":"Alpha-tubulin acetyltransferase\/MEC-17 regulates cancer cell migration and invasion through epithelial\u2013mesenchymal transition suppression and cell polarity disruption","volume":"8","author":"Lee","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_389","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1002\/ijc.32169","article-title":"Selective pharmacological inhibitors of HDAC6 reveal biochemical activity but functional tolerance in cancer models","volume":"145","author":"Depetter","year":"2019","journal-title":"Int. J. Cancer"},{"key":"ref_390","doi-asserted-by":"crossref","first-page":"e202205092","DOI":"10.1083\/jcb.202205092","article-title":"\u03b1-Tubulin detyrosination links the suppression of MCAK activity with taxol cytotoxicity","volume":"222","author":"Lopes","year":"2022","journal-title":"J. Cell Biol."},{"key":"ref_391","doi-asserted-by":"crossref","first-page":"2115","DOI":"10.1096\/fj.07-099671","article-title":"Molecular and cellular aspects of protein misfolding and disease","volume":"22","author":"Herczenik","year":"2008","journal-title":"FASEB J."},{"key":"ref_392","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1056\/NEJMra1106180","article-title":"Proteotoxicity and Cardiac Dysfunction\u2014Alzheimer\u2019s Disease of the Heart?","volume":"368","author":"Willis","year":"2013","journal-title":"N. Engl. J. Med."},{"key":"ref_393","doi-asserted-by":"crossref","unstructured":"Folger, A., and Wang, Y. (2021). The Cytotoxicity and Clearance of Mutant Huntingtin and Other Misfolded Proteins. Cells, 10.","DOI":"10.3390\/cells10112835"},{"key":"ref_394","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1161\/hh1301.092688","article-title":"Expression of R120G-\u03b1B-Crystallin Causes Aberrant Desmin and \u03b1B-Crystallin Aggregation and Cardiomyopathy in Mice","volume":"89","author":"Wang","year":"2001","journal-title":"Circ. Res."},{"key":"ref_395","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1161\/CIRCRESAHA.109.212639","article-title":"Manipulation of Death Pathways in Desmin-Related Cardiomyopathy","volume":"106","author":"Maloyan","year":"2010","journal-title":"Circ. Res."},{"key":"ref_396","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/nrcardio.2017.89","article-title":"Proteostasis in cardiac health and disease","volume":"14","author":"Henning","year":"2017","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_397","doi-asserted-by":"crossref","first-page":"10132","DOI":"10.1073\/pnas.0401900101","article-title":"Desmin-related cardiomyopathy in transgenic mice: A cardiac amyloidosis","volume":"101","author":"Sanbe","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_398","doi-asserted-by":"crossref","first-page":"E5178-86","DOI":"10.1073\/pnas.1415589111","article-title":"Tubulin hyperacetylation is adaptive in cardiac proteotoxicity by promoting autophagy","volume":"111","author":"McLendon","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_399","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1161\/CIRCULATIONAHA.113.005300","article-title":"Activation of Histone Deacetylase-6 Induces Contractile Dysfunction Through Derailment of \u03b1-Tubulin Proteostasis in Experimental and Human Atrial Fibrillation","volume":"129","author":"Zhang","year":"2014","journal-title":"Circulation"},{"key":"ref_400","doi-asserted-by":"crossref","first-page":"e00538-17","DOI":"10.1128\/JVI.00538-17","article-title":"Microtubule Regulation and Function during Virus Infection","volume":"91","author":"Naghavi","year":"2017","journal-title":"J. Virol."},{"key":"ref_401","doi-asserted-by":"crossref","unstructured":"Seo, D., and Gammon, D.B. (2022). Manipulation of Host Microtubule Networks by Viral Microtubule-Associated Proteins. Viruses, 14.","DOI":"10.3390\/v14050979"},{"key":"ref_402","doi-asserted-by":"crossref","first-page":"5445","DOI":"10.1091\/mbc.e05-04-0354","article-title":"Histone Deacetylase 6 Regulates Human Immunodeficiency Virus Type 1 Infection","volume":"16","author":"Gordon","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_403","doi-asserted-by":"crossref","first-page":"28800","DOI":"10.1074\/jbc.M702823200","article-title":"Regulation of Microtubule Assembly and Stability by the Transactivator of Transcription Protein of Jembrana Disease Virus","volume":"282","author":"Xuan","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_404","doi-asserted-by":"crossref","first-page":"6375","DOI":"10.1128\/JVI.02571-08","article-title":"The Hepatitis E Virus Open Reading Frame 3 Product Interacts with Microtubules and Interferes with Their Dynamics","volume":"83","author":"Kannan","year":"2009","journal-title":"J. Virol."},{"key":"ref_405","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.febslet.2010.11.023","article-title":"Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells","volume":"585","author":"Husain","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_406","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1099\/jgv.0.000679","article-title":"Cellular defence or viral assist: The dilemma of HDAC6","volume":"98","author":"Zheng","year":"2017","journal-title":"J. Gen. Virol."},{"key":"ref_407","doi-asserted-by":"crossref","first-page":"11229","DOI":"10.1128\/JVI.00727-14","article-title":"Histone Deacetylase 6 Inhibits Influenza A Virus Release by Downregulating the Trafficking of Viral Components to the Plasma Membrane via Its Substrate, Acetylated Microtubules","volume":"88","author":"Husain","year":"2014","journal-title":"J. Virol."},{"key":"ref_408","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1128\/JVI.79.2.1191-1206.2005","article-title":"Kaposi\u2019s Sarcoma-Associated Herpesvirus Modulates Microtubule Dynamics via RhoA-GTP-Diaphanous 2 Signaling and Utilizes the Dynein Motors To Deliver Its DNA to the Nucleus","volume":"79","author":"Naranatt","year":"2005","journal-title":"J. Virol."},{"key":"ref_409","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.chom.2013.10.012","article-title":"HIV-1 Induces the Formation of Stable Microtubules to Enhance Early Infection","volume":"14","author":"Sabo","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_410","doi-asserted-by":"crossref","first-page":"e01802-16","DOI":"10.1128\/JVI.01802-16","article-title":"Inclusion Body Fusion of Human Parainfluenza Virus Type 3 Regulated by Acetylated \u03b1-Tubulin Enhances Viral Replication","volume":"91","author":"Zhang","year":"2017","journal-title":"J. Virol."},{"key":"ref_411","doi-asserted-by":"crossref","unstructured":"Liu, P., Zhang, S., Ma, J., Jin, D., Qin, Y., and Chen, M. (2022). Vimentin inhibits \u03b1-tubulin acetylation via enhancing \u03b1-TAT1 degradation to suppress the replication of human parainfluenza virus type 3. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010856"},{"key":"ref_412","doi-asserted-by":"crossref","unstructured":"Glon, D., Vilmen, G., Perdiz, D., Hernandez, E., Beauclair, G., Quignon, F., Berlioz-Torrent, C., Mar\u00e9chal, V., Po\u00fcs, C., and Lussignol, M. (2022). Essential role of hyperacetylated microtubules in innate immunity escape orchestrated by the EBV-encoded BHRF1 protein. PLoS Pathog., 18.","DOI":"10.1101\/2021.06.11.448012"},{"key":"ref_413","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.1242\/jcs.02425","article-title":"A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts","volume":"118","author":"Destaing","year":"2005","journal-title":"J. Cell Sci."},{"key":"ref_414","doi-asserted-by":"crossref","first-page":"2047","DOI":"10.1091\/mbc.12.7.2047","article-title":"The Golgi Complex Is a Microtubule-organizing Organelle","volume":"12","author":"Marceiller","year":"2001","journal-title":"Mol. Biol. 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