{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T09:24:09Z","timestamp":1791365049216,"version":"4.3.1"},"reference-count":149,"publisher":"Elsevier BV","issue":"21","license":[{"start":{"date-parts":[[2022,11,1]],"date-time":"2022-11-01T00:00:00Z","timestamp":1667260800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,11,1]],"date-time":"2022-11-01T00:00:00Z","timestamp":1667260800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,11,7]],"date-time":"2023-11-07T00:00:00Z","timestamp":1699315200000},"content-version":"vor","delay-in-days":371,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Developmental Cell"],"published-print":{"date-parts":[[2022,11]]},"DOI":"10.1016\/j.devcel.2022.10.003","type":"journal-article","created":{"date-parts":[[2022,11,7]],"date-time":"2022-11-07T10:41:45Z","timestamp":1667817705000},"page":"2497-2513.e6","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":57,"title":["Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing"],"prefix":"10.1016","volume":"57","author":[{"given":"Ewa","family":"Szczesna","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena A.","family":"Zehr","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven W.","family":"Cummings","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Agnieszka","family":"Szyk","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kishore K.","family":"Mahalingan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonina","family":"Roll-Mecak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.devcel.2022.10.003_bib1","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1002\/cm.21679","article-title":"Posttranslational modifications of the cytoskeleton","volume":"78","author":"Mactaggart","year":"2021","journal-title":"Cytoskeleton (Hoboken)"},{"key":"10.1016\/j.devcel.2022.10.003_bib2","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","author":"Roll-Mecak","year":"2020","journal-title":"Dev. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib3","doi-asserted-by":"crossref","first-page":"135656","DOI":"10.1016\/j.neulet.2021.135656","article-title":"Tubulin polyglutamylation, a regulator of microtubule functions, can cause neurodegeneration","volume":"746","author":"Bodakuntla","year":"2021","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib4","first-page":"1","article-title":"Post-translational modifications of tubulin: their role in cancers and the regulation of signaling molecules","author":"Wattanathamsan","year":"2021","journal-title":"Cancer Gene Ther."},{"key":"10.1016\/j.devcel.2022.10.003_bib5","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1002\/(SICI)1097-0169(1997)37:1<72::AID-CM7>3.0.CO;2-J","article-title":"Purification and characterization of basal apparatuses from a flagellate green alga","volume":"37","author":"Geimer","year":"1997","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib6","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1016\/S0014-5793(98)00644-9","article-title":"Posttranslational modifications of trichomonad tubulins; identification of multiple glutamylation sites","volume":"429","author":"Schneider","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib7","doi-asserted-by":"crossref","first-page":"2981","DOI":"10.1021\/acschembio.6b00507","article-title":"Molecular determinants of tubulin\u2019s C-terminal tail conformational ensemble","volume":"11","author":"Wall","year":"2016","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib8","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1002\/(SICI)1097-0169(1998)41:4<341::AID-CM6>3.0.CO;2-8","article-title":"Expression of glycylated tubulin during the differentiation of spermatozoa in mammals","volume":"41","author":"Kann","year":"1998","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib9","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1111\/j.1768-322X.1999.tb01113.x","article-title":"Composition and organization of tubulin isoforms reveals a variety of axonemal models","volume":"91","author":"P\u00e9chart","year":"1999","journal-title":"Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib10","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1002\/1097-0169(200011)47:3<219::AID-CM5>3.0.CO;2-Q","article-title":"Distribution of polyglutamylated tubulin in the flagellar apparatus of green flagellates","volume":"47","author":"Lechtreck","year":"2000","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib11","doi-asserted-by":"crossref","first-page":"10862","DOI":"10.1021\/bi961057u","article-title":"The A and B tubules of the outer doublets\u00a0of sea urchin sperm axonemes are composed of different tubulin variants","volume":"35","author":"Multigner","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/j.devcel.2022.10.003_bib12","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":"10.1016\/j.devcel.2022.10.003_bib13","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":"2017","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib14","doi-asserted-by":"crossref","first-page":"3564","DOI":"10.1091\/mbc.e17-02-0124","article-title":"Tubulin isoform composition tunes microtubule dynamics","volume":"28","author":"Vemu","year":"2017","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib15","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0091-679X(10)95006-1","article-title":"Mass spectrometry analysis of C-terminal posttranslational modifications of tubulins","volume":"95","author":"Redeker","year":"2010","journal-title":"Methods Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib16","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":"2021","journal-title":"Dev. Neurobiol."},{"key":"10.1016\/j.devcel.2022.10.003_bib17","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1091\/mbc.e09-01-0044","article-title":"Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons","volume":"21","author":"Hammond","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib18","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1002\/cm.970120408","article-title":"Differential localisation of tyrosinated, detyrosinated, and acetylated \u03b1-tubulins in neurites and growth cones of dorsal root ganglion neurons","volume":"12","author":"Robson","year":"1989","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib19","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.67925","article-title":"Quantitative mapping of dense microtubule arrays in mammalian neurons","volume":"10","author":"Katrukha","year":"2021","journal-title":"eLife"},{"key":"10.1016\/j.devcel.2022.10.003_bib20","doi-asserted-by":"crossref","first-page":"2016","DOI":"10.1016\/j.devcel.2021.05.005","article-title":"\u03b1-tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics","volume":"56","author":"Chen","year":"2021","journal-title":"Dev. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib21","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1038\/s41586-021-04204-9","article-title":"ER proteins decipher the tubulin code to regulate organelle distribution","volume":"601","author":"Zheng","year":"2022","journal-title":"Nature"},{"key":"10.1016\/j.devcel.2022.10.003_bib22","doi-asserted-by":"crossref","first-page":"e108498","DOI":"10.15252\/embj.2021108498","article-title":"Distinct roles of \u03b1- and \u03b2-tubulin polyglutamylation in controlling axonal transport and in neurodegeneration","volume":"40","author":"Bodakuntla","year":"2021","journal-title":"EMBO J."},{"key":"10.1016\/j.devcel.2022.10.003_bib23","doi-asserted-by":"crossref","first-page":"2637","DOI":"10.1016\/j.celrep.2016.02.046","article-title":"\u03b1-tubulin tyrosination and CLIP-170 phosphorylation regulate the initiation of dynein-driven transport in neurons","volume":"14","author":"Nirschl","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.devcel.2022.10.003_bib24","doi-asserted-by":"crossref","DOI":"10.1126\/science.abd4914","article-title":"Tubulin glycylation controls axonemal dynein activity, flagellar beat, and male fertility","volume":"371","author":"Gadadhar","year":"2021","journal-title":"Science"},{"key":"10.1016\/j.devcel.2022.10.003_bib25","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":"10.1016\/j.devcel.2022.10.003_bib26","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/0092-8674(91)90511-V","article-title":"Severing of stable microtubules by a mitotically activated protein in Xenopus egg extracts","volume":"64","author":"Vale","year":"1991","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib27","doi-asserted-by":"crossref","first-page":"692040","DOI":"10.3389\/fcell.2021.692040","article-title":"The mammalian family of katanin microtubule-severing enzymes","volume":"9","author":"Lynn","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib28","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.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib29","doi-asserted-by":"crossref","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":"10.1016\/j.devcel.2022.10.003_bib30","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.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib31","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1242\/jcs.198010","article-title":"CAMSAP3 accumulates in the pericentrosomal area and accompanies microtubule release from the centrosome via katanin","volume":"130","author":"Dong","year":"2017","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib32","doi-asserted-by":"crossref","first-page":"5078","DOI":"10.1073\/pnas.94.10.5078","article-title":"Microtubule release from the centrosome","volume":"94","author":"Keating","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib33","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1038\/ncb2110","article-title":"Microtubule and katanin-dependent dynamics of microtubule nucleation complexes in the acentrosomal Arabidopsis cortical array","volume":"12","author":"Nakamura","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib34","doi-asserted-by":"crossref","first-page":"e202007167","DOI":"10.1083\/jcb.202007167","article-title":"WDR62 regulates spindle dynamics as an adaptor protein between TPX2\/Aurora A and katanin","volume":"220","author":"Huang","year":"2021","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib35","doi-asserted-by":"crossref","first-page":"1397","DOI":"10.1016\/j.cell.2011.11.014","article-title":"Katanin contributes to interspecies spindle length scaling in\u00a0Xenopus","volume":"147","author":"Loughlin","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib36","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1083\/jcb.200608117","article-title":"Katanin controls mitotic and meiotic spindle length","volume":"175","author":"McNally","year":"2006","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib37","doi-asserted-by":"crossref","first-page":"1072","DOI":"10.1101\/gad.14.9.1072","article-title":"MEI-1\/MEI-2 katanin-like microtubule severing activity is required for Caenorhabditis elegans meiosis","volume":"14","author":"Srayko","year":"2000","journal-title":"Genes Dev."},{"key":"10.1016\/j.devcel.2022.10.003_bib38","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1083\/jcb.200612011","article-title":"Three microtubule severing enzymes contribute to the \u201cPacMan-flux\u201d machinery that moves chromosomes","volume":"177","author":"Zhang","year":"2007","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib39","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1128\/EC.3.4.870-879.2004","article-title":"PF15p is the chlamydomonas homologue of the Katanin p80 subunit and is required for assembly of flagellar central microtubules","volume":"3","author":"Dymek","year":"2004","journal-title":"Eukaryot. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib40","first-page":"3357","article-title":"PF19 encodes the p60 catalytic subunit of katanin and is required for assembly of the flagellar central apparatus in Chlamydomonas","volume":"125","author":"Dymek","year":"2012","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib41","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.1016\/j.neuron.2014.12.017","article-title":"Katanin p80 regulates human cortical development by limiting centriole and cilia number","volume":"84","author":"Hu","year":"2014","journal-title":"Neuron"},{"key":"10.1016\/j.devcel.2022.10.003_bib42","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1083\/jcb.200704021","article-title":"Katanin regulates dynamics of microtubules and biogenesis of motile cilia","volume":"178","author":"Sharma","year":"2007","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib43","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202004184","article-title":"Katanin p60-like 1 sculpts the cytoskeleton in mechanosensory cilia","volume":"220","author":"Sun","year":"2021","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib44","doi-asserted-by":"crossref","first-page":"e3000381","DOI":"10.1371\/journal.pbio.3000381","article-title":"Primary cilium loss in mammalian cells occurs predominantly by whole-cilium shedding","volume":"17","author":"Mirvis","year":"2019","journal-title":"PLoS Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2019.01.020","article-title":"Structural and molecular basis for katanin-mediated severing of glutamylated microtubules","volume":"26","author":"Shin","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.devcel.2022.10.003_bib46","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1091\/mbc.e09-09-0834","article-title":"Basic fibroblast growth factor elicits formation of interstitial axonal branches via enhanced severing of microtubules","volume":"21","author":"Qiang","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib47","doi-asserted-by":"crossref","first-page":"6363","DOI":"10.1073\/pnas.0902051106","article-title":"Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamorphosis","volume":"106","author":"Lee","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib48","doi-asserted-by":"crossref","first-page":"11631","DOI":"10.1523\/JNEUROSCI.0729-12.2012","article-title":"Katanin p60-like1 promotes microtubule growth and terminal dendrite stability in the larval class IV sensory neurons of Drosophila","volume":"32","author":"Stewart","year":"2012","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.devcel.2022.10.003_bib49","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1002\/ajmg.a.36439","article-title":"A newly recognized 13q12.3 microdeletion syndrome characterized by intellectual disability, microcephaly, and eczema\/atopic dermatitis encompassing the HMGB1 and KATNAL1 genes","volume":"164A","author":"Bartholdi","year":"2014","journal-title":"Am. J. Med. Genet. A"},{"key":"10.1016\/j.devcel.2022.10.003_bib50","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.neuron.2014.12.046","article-title":"Mutations in KATNB1 cause complex cerebral malformations by disrupting asymmetrically dividing neural progenitors","volume":"85","author":"Mishra-Gorur","year":"2015","journal-title":"Neuron"},{"key":"10.1016\/j.devcel.2022.10.003_bib51","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1038\/ng.3792","article-title":"Targeted sequencing identifies 91 neurodevelopmental-disorder risk genes with autism and developmental-disability biases","volume":"49","author":"Stessman","year":"2017","journal-title":"Nat. Genet."},{"key":"10.1016\/j.devcel.2022.10.003_bib52","first-page":"4963","article-title":"The role of katanin p60 in breast cancer bone metastasis","volume":"15","author":"Fu","year":"2018","journal-title":"Oncol. Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib53","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.devcel.2019.10.010","article-title":"Katanin grips the beta-tubulin tail through an electropositive double spiral to sever microtubules","volume":"52","author":"Zehr","year":"2020","journal-title":"Dev. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib54","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cell.2004.09.020","article-title":"Sculpting the proteome with AAA+ proteases and disassembly machines","volume":"119","author":"Sauer","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib55","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a034033","article-title":"Spiraling in control: structures and mechanisms of the Hsp104 disaggregase","volume":"11","author":"Shorter","year":"2019","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib56","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1038\/ncb764","article-title":"Polyglycylation domain of\u00a0beta-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena","volume":"4","author":"Thazhath","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib57","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1002\/(SICI)1098-2795(199603)43:3<358::AID-MRD10>3.0.CO;2-Y","article-title":"Comparative immunogold analysis of tubulin isoforms in the mouse sperm flagellum: unique distribution of glutamylated tubulin","volume":"43","author":"Fouquet","year":"1996","journal-title":"Mol. Reprod. Dev."},{"key":"10.1016\/j.devcel.2022.10.003_bib58","article-title":"A key role for p60-katanin in axon navigation is conditioned by the tubulin polyglutamylase TTLL6","author":"Ten Martin","year":"2022","journal-title":"Preprint at bioRxiv"},{"key":"10.1016\/j.devcel.2022.10.003_bib59","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1083\/jcb.201001024","article-title":"Tubulin polyglutamylation stimulates spastin-mediated microtubule severing","volume":"189","author":"Lacroix","year":"2010","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib60","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1016\/j.cell.2016.01.019","article-title":"Graded control of microtubule severing by tubulin glutamylation","volume":"164","author":"Valenstein","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib61","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0092-8674(00)81578-0","article-title":"Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit","volume":"93","author":"Hartman","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib62","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":"Alexander","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib63","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1126\/science.1967194","article-title":"Posttranslational glutamylation of alpha-tubulin","volume":"247","author":"Edd\u00e9","year":"1990","journal-title":"Science"},{"key":"10.1016\/j.devcel.2022.10.003_bib64","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0014-5793(92)81441-N","article-title":"Structure of tubulin C-terminal domain obtained by subtilisin treatment. The major \u03b1 and \u03b2 tubulin isotypes from pig brain are glutamylated","volume":"313","author":"Redeker","year":"1992","journal-title":"FEBS Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib65","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":"R\u00fcdiger","year":"1992","journal-title":"FEBS Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib66","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/s41594-020-0462-0","article-title":"Structural basis\u00a0for polyglutamate chain initiation and elongation by TTLL family enzymes","volume":"27","author":"Mahalingan","year":"2020","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib67","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.molcel.2007.04.012","article-title":"A targeted multienzyme mechanism for selective microtubule polyglutamylation","volume":"26","author":"Van Dijk","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib68","doi-asserted-by":"crossref","first-page":"2313","DOI":"10.1242\/jcs.107.8.2313","article-title":"Developmental regulation of polyglutamylated alpha- and beta-tubulin in mouse brain neurons","volume":"107","author":"Audebert","year":"1994","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib69","doi-asserted-by":"crossref","first-page":"292","DOI":"10.3390\/cells9020292","article-title":"The LisH domain-containing N-terminal fragment is important for the localization, dimerization, and stability of Katnal2 in tetrahymena","volume":"9","author":"Joachimiak","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.devcel.2022.10.003_bib70","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1111\/mmi.13547","article-title":"Regulation of katanin activity in the ciliate Tetrahymena thermophila","volume":"103","author":"Waclawek","year":"2017","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.devcel.2022.10.003_bib71","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/B978-0-12-397924-7.00009-1","article-title":"Generation of differentially modified microtubules using in\u00a0vitro enzymatic approaches","volume":"540","author":"Vemu","year":"2014","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.devcel.2022.10.003_bib72","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/ng.1078","article-title":"CEP41 is mutated in Joubert syndrome and is required for tubulin glutamylation at the cilium","volume":"44","author":"Lee","year":"2012","journal-title":"Nat. Genet."},{"key":"10.1016\/j.devcel.2022.10.003_bib73","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1083\/jcb.201305041","article-title":"Tubulin glycylases and glutamylases have distinct functions in stabilization and motility of ependymal cilia","volume":"202","author":"Bosch Grau","year":"2013","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib74","doi-asserted-by":"crossref","first-page":"2706","DOI":"10.1016\/j.celrep.2017.08.063","article-title":"A mass spectrometry-based approach for mapping protein subcellular localization reveals the spatial proteome of mouse primary neurons","volume":"20","author":"Itzhak","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.devcel.2022.10.003_bib75","doi-asserted-by":"crossref","first-page":"e16950","DOI":"10.7554\/eLife.16950","article-title":"Global, quantitative and dynamic mapping of protein subcellular localization","volume":"5","author":"Itzhak","year":"2016","journal-title":"eLife"},{"key":"10.1016\/j.devcel.2022.10.003_bib76","doi-asserted-by":"crossref","first-page":"1847","DOI":"10.1091\/mbc.9.7.1847","article-title":"Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs","volume":"9","author":"McNally","year":"1998","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib77","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1126\/science.286.5440.782","article-title":"Microtubule disassembly by ATP-dependent oligomerization of the AAA enzyme katanin","volume":"286","author":"Hartman","year":"1999","journal-title":"Science"},{"key":"10.1016\/j.devcel.2022.10.003_bib78","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1016\/j.cell.2015.04.003","article-title":"Multivalent microtubule recognition by tubulin tyrosine ligase-like family glutamylases","volume":"161","author":"Garnham","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib79","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1021\/bi802047y","article-title":"Recombinant mammalian tubulin polyglutamylase TTLL7 performs both initiation and elongation of polyglutamylation on \u03b2-tubulin through a random sequential pathway","volume":"48","author":"Mukai","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.devcel.2022.10.003_bib80","doi-asserted-by":"crossref","first-page":"30707","DOI":"10.1074\/jbc.M603984200","article-title":"TTLL7 is a mammalian \u03b2-tubulin polyglutamylase required for growth of MAP2-positive neurites","volume":"281","author":"Ikegami","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib81","doi-asserted-by":"crossref","first-page":"6545","DOI":"10.1073\/pnas.1617286114","article-title":"Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases","volume":"114","author":"Garnham","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib82","doi-asserted-by":"crossref","first-page":"12907","DOI":"10.1074\/jbc.C116.731133","article-title":"Structure and dynamics of single-isoform recombinant neuronal human tubulin","volume":"291","author":"Vemu","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib83","first-page":"E6191","article-title":"Separating the effects of nucleotide and EB binding on microtubule structure","volume":"115","author":"Zhang","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib84","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.15252\/embj.201593071","article-title":"Tyrosination of \u03b1-tubulin controls the initiation of processive dynein\u2013dynactin motility","volume":"35","author":"McKenney","year":"2016","journal-title":"EMBO J."},{"key":"10.1016\/j.devcel.2022.10.003_bib85","doi-asserted-by":"crossref","first-page":"1159","DOI":"10.1083\/jcb.200902142","article-title":"Motor-dependent microtubule disassembly driven by tubulin tyrosination","volume":"185","author":"Peris","year":"2009","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib86","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/ncb2920","article-title":"Regulation of microtubule motors by tubulin isotypes and post-translational modifications","volume":"16","author":"Sirajuddin","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib87","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1083\/jcb.200512058","article-title":"Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends","volume":"174","author":"Peris","year":"2006","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib88","doi-asserted-by":"crossref","first-page":"1448","DOI":"10.1126\/science.aao4165","article-title":"Vasohibins\/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation","volume":"358","author":"Aillaud","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.devcel.2022.10.003_bib89","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1126\/science.aao5676","article-title":"Vasohibins encode tubulin detyrosinating activity","volume":"358","author":"Nieuwenhuis","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.devcel.2022.10.003_bib90","doi-asserted-by":"crossref","DOI":"10.1016\/j.str.2019.07.002","article-title":"Crystal structure of a heterotetrameric katanin p60: p80 complex","volume":"27","author":"Faltova","year":"2019","journal-title":"Structure"},{"key":"10.1016\/j.devcel.2022.10.003_bib91","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1038\/ncb3511","article-title":"Microtubule minus-end regulation at spindle poles by an ASPM\u2013katanin complex","volume":"19","author":"Jiang","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib92","doi-asserted-by":"crossref","first-page":"1623","DOI":"10.1242\/jcs.113.9.1623","article-title":"Two domains of p80 katanin regulate microtubule severing and spindle pole targeting by p60 katanin","volume":"113","author":"McNally","year":"2000","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib93","doi-asserted-by":"crossref","first-page":"14893","DOI":"10.1038\/s41598-017-14194-2","article-title":"Structural basis of katanin p60: p80 complex formation","volume":"7","author":"Rezabkova","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.devcel.2022.10.003_bib94","doi-asserted-by":"crossref","first-page":"2546","DOI":"10.1016\/j.bpj.2015.11.011","article-title":"Katanin severing and binding microtubules are inhibited by tubulin carboxy tails","volume":"109","author":"Bailey","year":"2015","journal-title":"Biophys. J."},{"key":"10.1016\/j.devcel.2022.10.003_bib95","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib96","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1002\/cm.970270106","article-title":"Differential distribution of glutamylated tubulin during spermatogenesis in mammalian testis","volume":"27","author":"Fouquet","year":"1994","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib97","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1083\/jcb.105.5.2167","article-title":"Posttranslational modification and microtubule stability","volume":"105","author":"Schulze","year":"1987","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib98","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.\u00a0Neurosci."},{"key":"10.1016\/j.devcel.2022.10.003_bib99","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":"Eshun-Wilson","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.devcel.2022.10.003_bib100","doi-asserted-by":"crossref","first-page":"e48204","DOI":"10.1371\/journal.pone.0048204","article-title":"Luminal localization of \u03b1-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules","volume":"7","author":"Soppina","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.devcel.2022.10.003_bib101","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":"10.1016\/j.devcel.2022.10.003_bib102","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1038\/ncb3481","article-title":"Tubulin acetylation protects long-lived microtubules against mechanical ageing","volume":"19","author":"Portran","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib103","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":"10.1016\/j.devcel.2022.10.003_bib104","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.jmb.2017.01.001","article-title":"Insights into the distinct mechanisms of action of taxane and non-taxane microtubule stabilizers from cryo-EM structures","volume":"429","author":"Kellogg","year":"2017","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib105","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1002\/cm.10080","article-title":"Katanin-mediated microtubule severing can be regulated by multiple mechanisms","volume":"53","author":"McNally","year":"2002","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.devcel.2022.10.003_bib106","doi-asserted-by":"crossref","first-page":"3120","DOI":"10.1523\/JNEUROSCI.5392-05.2006","article-title":"Tau protects microtubules in the axon from severing by katanin","volume":"26","author":"Qiang","year":"2006","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.devcel.2022.10.003_bib107","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1038\/s41556-019-0374-6","article-title":"Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes","volume":"21","author":"Siahaan","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib108","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":"10.1016\/j.devcel.2022.10.003_bib109","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":"10.1016\/j.devcel.2022.10.003_bib110","doi-asserted-by":"crossref","first-page":"1957","DOI":"10.1016\/j.febslet.2009.05.003","article-title":"TTLL10 can perform tubulin glycylation when co-expressed with TTLL8","volume":"583","author":"Ikegami","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.devcel.2022.10.003_bib111","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1002\/cm.21027","article-title":"The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions","volume":"69","author":"Garnham","year":"2012","journal-title":"Cytoskeleton (Hoboken)"},{"key":"10.1016\/j.devcel.2022.10.003_bib112","doi-asserted-by":"crossref","first-page":"6530","DOI":"10.1039\/D2CC01783K","article-title":"Phosphinic acid-based inhibitors of tubulin polyglycylation","volume":"58","author":"Zhuang","year":"2022","journal-title":"Chem. Commun. (Camb)"},{"key":"10.1016\/j.devcel.2022.10.003_bib113","doi-asserted-by":"crossref","first-page":"5796","DOI":"10.1038\/s41467-021-26058-5","article-title":"Wdr47, Camsaps, and Katanin cooperate to generate ciliary central microtubules","volume":"12","author":"Liu","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.devcel.2022.10.003_bib114","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.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib115","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":"10.1016\/j.devcel.2022.10.003_bib116","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1074\/jbc.AC119.009890","article-title":"Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation","volume":"295","author":"Han","year":"2020","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib117","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/s41594-019-0257-3","article-title":"An allosteric network in spastin couples multiple activities required for microtubule severing","volume":"26","author":"Sandate","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib118","doi-asserted-by":"crossref","first-page":"e44071","DOI":"10.7554\/eLife.44071","article-title":"Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases","volume":"8","author":"Han","year":"2019","journal-title":"eLife"},{"key":"10.1016\/j.devcel.2022.10.003_bib119","doi-asserted-by":"crossref","DOI":"10.1016\/j.cell.2017.04.020","article-title":"Molecular mechanism of substrate processing by the Cdc48 ATPase complex","volume":"169","author":"Bodnar","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib120","doi-asserted-by":"crossref","first-page":"3092","DOI":"10.1093\/emboj\/20.12.3092","article-title":"Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine","volume":"20","author":"Burton","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.devcel.2022.10.003_bib121","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1021\/cb2002285","article-title":"Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization","volume":"6","author":"Kraut","year":"2011","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib122","doi-asserted-by":"crossref","first-page":"34760","DOI":"10.1074\/jbc.M204750200","article-title":"Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel","volume":"277","author":"Lee","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib123","doi-asserted-by":"crossref","first-page":"e100440","DOI":"10.15252\/embj.2018100440","article-title":"Excessive tubulin polyglutamylation causes neurodegeneration and perturbs neuronal transport","volume":"37","author":"Magiera","year":"2018","journal-title":"EMBO J."},{"key":"10.1016\/j.devcel.2022.10.003_bib124","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.semcdb.2014.09.026","article-title":"Intrinsically disordered tubulin tails: complex tuners of microtubule functions?","volume":"37","author":"Roll-Mecak","year":"2015","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib125","doi-asserted-by":"crossref","first-page":"7380","DOI":"10.1021\/ja710446s","article-title":"Role of backbone\u2212 solvent interactions in determining conformational equilibria of intrinsically disordered proteins","volume":"130","author":"Tran","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.devcel.2022.10.003_bib126","doi-asserted-by":"crossref","first-page":"166988","DOI":"10.1016\/j.jmb.2021.166988","article-title":"Modulating microtubules: A molecular perspective on the effects of tail modifications","volume":"433","author":"Bigman","year":"2021","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib127","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1074\/jbc.M408324200","article-title":"Mutations of tubulin glycylation sites reveal cross-talk between the C termini of \u03b1- and \u03b2-tubulin and affect the ciliary matrix in Tetrahymena","volume":"280","author":"Redeker","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib128","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1002\/dvdy.24599","article-title":"ReMAPping the microtubule landscape: how phosphorylation dictates the activities of microtubule-associated proteins","volume":"247","author":"Ramkumar","year":"2018","journal-title":"Dev. Dyn."},{"key":"10.1016\/j.devcel.2022.10.003_bib129","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.tibs.2008.08.006","article-title":"Capturing protein tails by CAP-Gly domains","volume":"33","author":"Steinmetz","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib130","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1074\/mcp.M115.056465","article-title":"Proteomic analysis of the mammalian katanin family of microtubule-severing enzymes defines katanin p80 subunit B-like 1 (KATNBL1) as a regulator of mammalian katanin microtubule-severing","volume":"15","author":"Cheung","year":"2016","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.devcel.2022.10.003_bib131","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/nsmb.3448","article-title":"Katanin spiral and ring structures shed light on power stroke for microtubule severing","volume":"24","author":"Zehr","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib132","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1083\/jcb.201412097","article-title":"Glutamylation of Nap1 modulates histone H1 dynamics and chromosome condensation in Xenopus","volume":"209","author":"Miller","year":"2015","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib133","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/ni.3356","article-title":"Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity","volume":"17","author":"Xia","year":"2016","journal-title":"Nat. Immunol."},{"key":"10.1016\/j.devcel.2022.10.003_bib134","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1083\/jcb.149.5.1097","article-title":"Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila","volume":"149","author":"Xia","year":"2000","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib135","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1091\/mbc.e13-12-0764","article-title":"Katanin maintains meiotic metaphase chromosome alignment and spindle structure in\u00a0vivo and has multiple effects on microtubules in\u00a0vitro","volume":"25","author":"McNally","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib136","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1038\/nmeth.2019","article-title":"Fiji: an open-source platform for biological-image analysis","volume":"9","author":"Schindelin","year":"2012","journal-title":"Nat. Methods"},{"key":"10.1016\/j.devcel.2022.10.003_bib137","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.devcel.2022.10.003_bib138","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1107\/S0907444909029436","article-title":"Electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation","volume":"65","author":"Moriarty","year":"2009","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.devcel.2022.10.003_bib139","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1002\/pro.3235","article-title":"UCSF ChimeraX: meeting modern challenges in visualization and analysis","volume":"27","author":"Goddard","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.devcel.2022.10.003_bib140","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.devcel.2022.10.003_bib141","series-title":"PhysiologyMOL molecular graphics system, version 1.8","year":"2015"},{"key":"10.1016\/j.devcel.2022.10.003_bib142","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1038\/nprot.2013.102","article-title":"Site-specific N-terminal labeling of proteins using sortase-mediated reactions","volume":"8","author":"Theile","year":"2013","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.devcel.2022.10.003_bib143","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1472-6750-13-12","article-title":"A new method to customize protein expression vectors for fast, efficient and background free parallel cloning","volume":"13","author":"Scholz","year":"2013","journal-title":"BMC Biotechnol."},{"key":"10.1016\/j.devcel.2022.10.003_bib144","doi-asserted-by":"crossref","first-page":"4393","DOI":"10.1091\/mbc.e12-06-0444","article-title":"One-step purification of assembly-competent tubulin from diverse eukaryotic sources","volume":"23","author":"Widlund","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.devcel.2022.10.003_bib145","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S1046-5928(03)00218-3","article-title":"Purification of brain tubulin through two cycles of polymerization\u2013depolymerization in a high-molarity buffer","volume":"32","author":"Castoldi","year":"2003","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.devcel.2022.10.003_bib146","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1007\/978-1-62703-538-5_19","article-title":"In\u00a0vitro microtubule severing assays","volume":"1046","author":"Zi\u00f3\u0142kowska","year":"2013","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib147","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"Phenix: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.devcel.2022.10.003_bib148","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1107\/S2059798318006551","article-title":"Real-space refinement in PHENIX for cryo-EM and crystallography","volume":"74","author":"Afonine","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.devcel.2022.10.003_bib149","doi-asserted-by":"crossref","first-page":"W368","DOI":"10.1093\/nar\/gky309","article-title":"MOLEonline: a web-based tool for analyzing channels, tunnels and pores (2018 update)","volume":"46","author":"Pravda","year":"2018","journal-title":"Nucleic Acids Res."}],"container-title":["Developmental Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1534580722007225?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1534580722007225?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T23:45:37Z","timestamp":1761522337000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1534580722007225"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11]]},"references-count":149,"journal-issue":{"issue":"21","published-print":{"date-parts":[[2022,11]]}},"alternative-id":["S1534580722007225"],"URL":"https:\/\/doi.org\/10.1016\/j.devcel.2022.10.003","relation":{},"ISSN":["1534-5807"],"issn-type":[{"value":"1534-5807","type":"print"}],"subject":[],"published":{"date-parts":[[2022,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing","name":"articletitle","label":"Article Title"},{"value":"Developmental Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.devcel.2022.10.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}