{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T20:01:58Z","timestamp":1791576118802,"version":"4.3.4"},"reference-count":87,"publisher":"Elsevier BV","issue":"28","license":[{"start":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T00:00:00Z","timestamp":1372636800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,7]],"date-time":"2020-09-07T00:00:00Z","timestamp":1599436800000},"content-version":"vor","delay-in-days":2625,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,7]]},"DOI":"10.1074\/jbc.m113.464792","type":"journal-article","created":{"date-parts":[[2013,5,29]],"date-time":"2013-05-29T00:24:33Z","timestamp":1369787073000},"page":"20334-20350","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":148,"title":["Mice Lacking \u03b1-Tubulin Acetyltransferase 1 Are Viable but Display \u03b1-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion"],"prefix":"10.1016","volume":"288","author":[{"given":"Go-Woon","family":"Kim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lin","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad","family":"Gorbani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Linya","family":"You","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang-Jiao","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.464792_bib1","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1093\/emboj\/19.6.1176","article-title":"Acetylation: a regulatory modification to rival phosphorylation?","volume":"19","author":"Kouzarides","year":"2000","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M113.464792_bib2","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.molcel.2008.07.002","article-title":"Lysine acetylation: codified crosstalk with other posttranslational modifications","volume":"31","author":"Yang","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.464792_bib3","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.cell.2012.05.036","article-title":"Systematic functional prioritization of protein posttranslational modifications","volume":"150","author":"Beltrao","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib4","doi-asserted-by":"crossref","first-page":"786","DOI":"10.1073\/pnas.51.5.786","article-title":"Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis","volume":"51","author":"Allfrey","year":"1964","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib5","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/47412","article-title":"The language of covalent histone modifications","volume":"403","author":"Strahl","year":"2000","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.464792_bib6","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2007.02.005","article-title":"Chromatin modifications and their function","volume":"128","author":"Kouzarides","year":"2007","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib7","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nature05915","article-title":"The complex language of chromatin regulation during transcription","volume":"447","author":"Berger","year":"2007","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.464792_bib8","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1038\/nsmb1307","article-title":"Cross-regulation of histone modifications","volume":"14","author":"Latham","year":"2007","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.464792_bib9","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1016\/j.molcel.2006.06.026","article-title":"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey","volume":"23","author":"Kim","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.464792_bib10","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":"10.1074\/jbc.M113.464792_bib11","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1126\/science.1179689","article-title":"Regulation of cellular metabolism by protein lysine acetylation","volume":"327","author":"Zhao","year":"2010","journal-title":"Science"},{"key":"10.1074\/jbc.M113.464792_bib12","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.cell.2012.02.064","article-title":"Exploring the yeast acetylome using functional genomics","volume":"149","author":"Kaluarachchi Duffy","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib13","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M800187-MCP200","article-title":"Lysine acetylation is a highly abundant and evolutionarily conserved modification in","volume":"8","author":"Zhang","year":"2009","journal-title":"Escherichia coli. Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.M113.464792_bib14","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1126\/science.1179687","article-title":"Acetylation of metabolic enzymes coordinates carbon source utilization and metabolic flux","volume":"327","author":"Wang","year":"2010","journal-title":"Science"},{"key":"10.1074\/jbc.M113.464792_bib15","doi-asserted-by":"crossref","first-page":"5310","DOI":"10.1038\/sj.onc.1210599","article-title":"HATs and HDACs: from structure, function, and regulation to novel strategies for therapy and prevention","volume":"26","author":"Yang","year":"2007","journal-title":"Oncogene"},{"key":"10.1074\/jbc.M113.464792_bib16","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/j.cell.2007.10.039","article-title":"New nomenclature for chromatin-modifying enzymes","volume":"131","author":"Allis","year":"2007","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib17","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1038\/nrm2145","article-title":"Histone acetyltransferase complexes: one size doesn't fit all","volume":"8","author":"Lee","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib18","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/S0959-437X(00)00174-X","article-title":"Functional significance of histone deacetylase diversity","volume":"11","author":"Khochbin","year":"2001","journal-title":"Curr. Opin. Genet. Dev"},{"key":"10.1074\/jbc.M113.464792_bib19","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S1074-5521(02)00092-3","article-title":"Deacetylase enzymes: biological functions and the use of small-molecule inhibitors","volume":"9","author":"Grozinger","year":"2002","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.M113.464792_bib20","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/S0168-9525(03)00073-8","article-title":"Class II histone deacetylases: versatile regulators","volume":"19","author":"Verdin","year":"2003","journal-title":"Trends Genet"},{"key":"10.1074\/jbc.M113.464792_bib21","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1038\/nrm2346","article-title":"The Rpd3\/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men","volume":"9","author":"Yang","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib22","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/nrg2485","article-title":"The many roles of histone deacetylases in development and physiology: implications for disease and therapy","volume":"10","author":"Haberland","year":"2009","journal-title":"Nat. Rev. Genet"},{"key":"10.1074\/jbc.M113.464792_bib23","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1038\/nrm1260","article-title":"Post-translational modifications regulate microtubule function","volume":"4","author":"Westermann","year":"2003","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib24","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1038\/nrm3227","article-title":"Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions","volume":"12","author":"Janke","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib25","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1021\/bi00323a034","article-title":"Chlamydomonas \u03b1-tubulin is posttranslationally modified by acetylation on the \u03f5-amino group of a lysine","volume":"24","author":"L'Hernault","year":"1985","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.464792_bib26","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1083\/jcb.101.6.2085","article-title":"Monoclonal antibodies specific for an acetylated form of \u03b1-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":"10.1074\/jbc.M113.464792_bib27","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1083\/jcb.104.2.289","article-title":"Microtubules containing acetylated \u03b1-tubulin in mammalian cells in culture","volume":"104","author":"Piperno","year":"1987","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib28","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1073\/pnas.84.16.5720","article-title":"Identification of an acetylation site of Chlamydomonas \u03b1-tubulin","volume":"84","author":"LeDizet","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib29","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":"10.1074\/jbc.M113.464792_bib30","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/421230a","article-title":"Cell biology: tubulin acetylation and cell motility","volume":"421","author":"Palazzo","year":"2003","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.464792_bib31","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":"10.1074\/jbc.M113.464792_bib32","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. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib33","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":"10.1074\/jbc.M113.464792_bib34","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":"10.1074\/jbc.M113.464792_bib35","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's disease by increasing tubulin acetylation","volume":"27","author":"Dompierre","year":"2007","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.464792_bib36","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1083\/jcb.200707042","article-title":"Microtubule stabilization specifies initial neuronal polarization","volume":"180","author":"Witte","year":"2008","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib37","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":"10.1074\/jbc.M113.464792_bib38","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":"10.1074\/jbc.M113.464792_bib39","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1083\/jcb.129.5.1301","article-title":"Acetylation of lysine 40 in \u03b1-tubulin is not essential in Tetrahymena thermophila","volume":"129","author":"Gaertig","year":"1995","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib40","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1002\/cm.970250205","article-title":"High level expression of nonacetylatable \u03b1-tubulin in Chlamydomonas reinhardtii","volume":"25","author":"Kozminski","year":"1993","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1074\/jbc.M113.464792_bib41","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1242\/jcs.112.3.395","article-title":"MEC-12, an \u03b1-tubulin required for touch sensitivity in C. elegans","volume":"112","author":"Fukushige","year":"1999","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.M113.464792_bib42","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1111\/jipb.12003","article-title":"A single amino-acid substitution at lysine 40 of an Arabidopsis thaliana \u03b1-tubulin causes extensive cell proliferation and expansion defects","volume":"55","author":"Xiong","year":"2013","journal-title":"J. Integr. Plant Biol"},{"key":"10.1074\/jbc.M113.464792_bib43","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":"10.1074\/jbc.M113.464792_bib44","doi-asserted-by":"crossref","first-page":"12673","DOI":"10.1523\/JNEUROSCI.0016-12.2012","article-title":"MEC-17 deficiency leads to reduced \u03b1-tubulin acetylation and impaired migration of cortical neurons","volume":"32","author":"Li","year":"2012","journal-title":"J. Neurosci"},{"key":"10.1074\/jbc.M113.464792_bib45","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":"10.1074\/jbc.M113.464792_bib46","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":"10.1074\/jbc.M113.464792_bib47","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":"10.1074\/jbc.M113.464792_bib48","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":"10.1074\/jbc.M113.464792_bib49","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":"10.1074\/jbc.M113.464792_bib50","doi-asserted-by":"crossref","first-page":"e34805","DOI":"10.1371\/journal.pone.0034805","article-title":"SIRT2 ablation has no effect on tubulin acetylation in brain, cholesterol biosynthesis, or the progression of Huntington's disease phenotypes in vivo","volume":"7","author":"Bobrowska","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M113.464792_bib51","doi-asserted-by":"crossref","first-page":"e30924","DOI":"10.1371\/journal.pone.0030924","article-title":"Loss of deacetylation activity of Hdac6 affects emotional behavior in mice","volume":"7","author":"Fukada","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.M113.464792_bib52","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":"10.1074\/jbc.M113.464792_bib53","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":"10.1074\/jbc.M113.464792_bib54","doi-asserted-by":"crossref","first-page":"e1000820","DOI":"10.1371\/journal.pgen.1000820","article-title":"The Caenorhabditis elegans elongator complex regulates neuronal \u03b1-tubulin acetylation","volume":"6","author":"Solinger","year":"2010","journal-title":"PLoS Genet"},{"key":"10.1074\/jbc.M113.464792_bib55","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":"Conacci-Sorrell","year":"2010","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib56","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":"10.1074\/jbc.M113.464792_bib57","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":"10.1074\/jbc.M113.464792_bib58","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":"10.1074\/jbc.M113.464792_bib59","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. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib60","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. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib61","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nrg2774","article-title":"The primary cilium: a signalling centre during vertebrate development","volume":"11","author":"Goetz","year":"2010","journal-title":"Nat. Rev. Genet"},{"key":"10.1074\/jbc.M113.464792_bib62","series-title":"Manipulating the Mouse Embryo","author":"Nagy","year":"2003"},{"key":"10.1074\/jbc.M113.464792_bib63","doi-asserted-by":"crossref","first-page":"5591","DOI":"10.1074\/jbc.M112.445668","article-title":"Dephosphorylation at a conserved SP motif governs cAMP sensitivity and nuclear localization of class IIa histone deacetylases","volume":"288","author":"Walkinshaw","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464792_bib64","doi-asserted-by":"crossref","first-page":"3081","DOI":"10.1038\/nprot.2007.418","article-title":"Induction of pluripotent stem cells from fibroblast cultures","volume":"2","author":"Takahashi","year":"2007","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.M113.464792_bib65","doi-asserted-by":"crossref","first-page":"12791","DOI":"10.1074\/jbc.M113.465443","article-title":"Sumoylation of Kruppel-like factor 4 inhibits pluripotency induction but promotes adipocyte differentiation","volume":"288","author":"Tahmasebi","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464792_bib66","doi-asserted-by":"crossref","first-page":"9345","DOI":"10.1074\/jbc.M113.456996","article-title":"The tumor suppressor kinase LKB1 activates the downstream kinases SIK2 and SIK3 to stimulate nuclear export of class IIa histone deacetylases","volume":"288","author":"Walkinshaw","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.464792_bib67","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1083\/jcb.103.1.13","article-title":"Cytoplasmic microtubules containing acetylated \u03b1-tubulin in Chlamydomonas reinhardtii: spatial arrangement and properties","volume":"103","author":"LeDizet","year":"1986","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib68","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1083\/jcb.111.2.495","article-title":"Individual microtubules in the axon consist of domains that differ in both composition and stability","volume":"111","author":"Baas","year":"1990","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib69","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1083\/jcb.127.5.1407","article-title":"The initiation of neurite outgrowth by sympathetic neurons grown in vitro does not depend on assembly of microtubules","volume":"127","author":"Smith","year":"1994","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.464792_bib70","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1111\/j.1471-4159.2009.06013.x","article-title":"Post-translational modifications of tubulin in the nervous system","volume":"109","author":"Fukushima","year":"2009","journal-title":"J. Neurochem"},{"key":"10.1074\/jbc.M113.464792_bib71","series-title":"Allen Reference Atlas, A Digital Brain Atlas of the C57BL\/6J Male Mouse","author":"Dong","year":"2008"},{"key":"10.1074\/jbc.M113.464792_bib72","series-title":"The Mouse Brain in Stereotaxic Coordinates","author":"Paxinos","year":"2008"},{"key":"10.1074\/jbc.M113.464792_bib73","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1126\/science.1361685","article-title":"Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice","volume":"258","author":"Grant","year":"1992","journal-title":"Science"},{"key":"10.1074\/jbc.M113.464792_bib74","doi-asserted-by":"crossref","first-page":"4761","DOI":"10.1073\/pnas.94.9.4761","article-title":"Rescuing impairment of long-term potentiation in fyn-deficient mice by introducing Fyn transgene","volume":"94","author":"Kojima","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.464792_bib75","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1128\/MCB.01044-12","article-title":"The tubulin acetyltransferase \u03b1TAT1 destabilizes microtubules independently of its acetylation activity","volume":"33","author":"Kalebic","year":"2013","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M113.464792_bib76","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/j.cell.2008.01.033","article-title":"Mechanisms and functional implications of adult neurogenesis","volume":"132","author":"Zhao","year":"2008","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib77","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0896-6273(00)80777-1","article-title":"Doublecortin is a developmentally regulated, microtubule-associated protein expressed in migrating and differentiating neurons","volume":"23","author":"Francis","year":"1999","journal-title":"Neuron"},{"key":"10.1074\/jbc.M113.464792_bib78","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0896-6273(00)80778-3","article-title":"Doublecortin is a microtubule-associated protein and is expressed widely by migrating neurons","volume":"23","author":"Gleeson","year":"1999","journal-title":"Neuron"},{"key":"10.1074\/jbc.M113.464792_bib79","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1038\/35016083","article-title":"Induction of neurogenesis in the neocortex of adult mice","volume":"405","author":"Magavi","year":"2000","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.464792_bib80","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0092-8674(00)80898-3","article-title":"A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome","volume":"92","author":"des Portes","year":"1998","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib81","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0092-8674(00)80899-5","article-title":"Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein","volume":"92","author":"Gleeson","year":"1998","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.464792_bib82","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.molcel.2004.06.009","article-title":"Mechanism of microtubule stabilization by doublecortin","volume":"14","author":"Moores","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.464792_bib83","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":"10.1074\/jbc.M113.464792_bib84","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":"10.1074\/jbc.M113.464792_bib85","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1126\/science.1201148","article-title":"Microtubule stabilization reduces scarring and causes axon regeneration after spinal cord injury","volume":"331","author":"Hellal","year":"2011","journal-title":"Science"},{"key":"10.1074\/jbc.M113.464792_bib86","doi-asserted-by":"crossref","first-page":"391","DOI":"10.4161\/cib.15552","article-title":"Facilitating axon regeneration in the injured CNS by microtubules stabilization","volume":"4","author":"Sengottuvel","year":"2011","journal-title":"Commun. Integr. Biol"},{"key":"10.1074\/jbc.M113.464792_bib87","doi-asserted-by":"crossref","first-page":"32888","DOI":"10.1074\/jbc.M110.162743","article-title":"Clostridium difficile toxin A decreases acetylation of tubulin, leading to microtubule depolymerization through activation of histone deacetylase 6, and this mediates acute inflammation","volume":"285","author":"Nam","year":"2010","journal-title":"J. Biol. Chem"}],"updated-by":[{"DOI":"10.1074\/jbc.a113.464792","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2016,11,25]],"date-time":"2016-11-25T00:00:00Z","timestamp":1480032000000}}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820456042?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820456042?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.464792","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,3]],"date-time":"2023-11-03T19:33:04Z","timestamp":1699039984000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820456042"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,7]]},"references-count":87,"journal-issue":{"issue":"28","published-print":{"date-parts":[[2013,7]]}},"alternative-id":["S0021925820456042"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.464792","relation":{"correction":[{"id-type":"doi","id":"10.1074\/jbc.A113.464792","asserted-by":"object"}]},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Mice Lacking \u03b1-Tubulin Acetyltransferase 1 Are Viable but Display \u03b1-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M113.464792","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}