{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,11]],"date-time":"2026-10-11T02:21:02Z","timestamp":1791685262048,"version":"4.3.4"},"reference-count":32,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2013,4,28]],"date-time":"2013-04-28T00:00:00Z","timestamp":1367107200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2013,6]]},"DOI":"10.1038\/nsmb.2555","type":"journal-article","created":{"date-parts":[[2013,4,28]],"date-time":"2013-04-28T18:15:34Z","timestamp":1367172934000},"page":"756-762","source":"Crossref","is-referenced-by-count":147,"title":["The microtubule-associated tau protein has intrinsic acetyltransferase activity"],"prefix":"10.1038","volume":"20","author":[{"given":"Todd J","family":"Cohen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dave","family":"Friedmann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew W","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronen","family":"Marmorstein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Virginia M Y","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2013,4,28]]},"reference":[{"key":"BFnsmb2555_CR1","doi-asserted-by":"publisher","first-page":"10626","DOI":"10.1021\/bi00158a027","volume":"31","author":"A Andreadis","year":"1992","unstructured":"Andreadis, A., Brown, W.M. & Kosik, K.S. Structure and novel exons of the human tau gene. Biochemistry 31, 10626\u201310633 (1992).","journal-title":"Biochemistry"},{"key":"BFnsmb2555_CR2","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/0896-6273(89)90210-9","volume":"3","author":"M Goedert","year":"1989","unstructured":"Goedert, M., Spillantini, M.G., Jakes, R., Rutherford, D. & Crowther, R.A. Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3, 519\u2013526 (1989).","journal-title":"Neuron"},{"key":"BFnsmb2555_CR3","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1111\/j.1749-6632.1996.tb34408.x","volume":"777","author":"VM Lee","year":"1996","unstructured":"Lee, V.M. Regulation of tau phosphorylation in Alzheimer's disease. Ann. NY Acad. Sci. 777, 107\u2013113 (1996).","journal-title":"Ann. NY Acad. Sci."},{"key":"BFnsmb2555_CR4","doi-asserted-by":"publisher","first-page":"1121","DOI":"10.1146\/annurev.neuro.24.1.1121","volume":"24","author":"VM Lee","year":"2001","unstructured":"Lee, V.M., Goedert, M. & Trojanowski, J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 24, 1121\u20131159 (2001).","journal-title":"Annu. Rev. Neurosci."},{"key":"BFnsmb2555_CR5","doi-asserted-by":"publisher","first-page":"252","DOI":"10.1038\/ncomms1255","volume":"2","author":"TJ Cohen","year":"2011","unstructured":"Cohen, T.J. et al. The acetylation of tau inhibits its function and promotes pathological tau aggregation. Nat. Commun. 2, 252 (2011).","journal-title":"Nat. Commun."},{"key":"BFnsmb2555_CR6","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1093\/brain\/aws013","volume":"135","author":"DJ Irwin","year":"2012","unstructured":"Irwin, D.J. et al. Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies. Brain 135, 807\u2013818 (2012).","journal-title":"Brain"},{"key":"BFnsmb2555_CR7","doi-asserted-by":"publisher","first-page":"953","DOI":"10.1016\/j.neuron.2010.08.044","volume":"67","author":"SW Min","year":"2010","unstructured":"Min, S.W. et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron 67, 953\u2013966 (2010).","journal-title":"Neuron"},{"key":"BFnsmb2555_CR8","doi-asserted-by":"publisher","first-page":"6364","DOI":"10.1073\/pnas.92.14.6364","volume":"92","author":"JE Brownell","year":"1995","unstructured":"Brownell, J.E. & Allis, C.D. An activity gel assay detects a single, catalytically active histone acetyltransferase subunit in Tetrahymena macronuclei. Proc. Natl. Acad. Sci. USA 92, 6364\u20136368 (1995).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2555_CR9","first-page":"343","volume":"119","author":"JE Brownell","year":"1999","unstructured":"Brownell, J.E., Mizzen, C.A. & Allis, C.D. An SDS-PAGE-based enzyme activity assay for the detection and identification of histone acetyltransferases. Methods Mol. Biol. 119, 343\u2013353 (1999).","journal-title":"Methods Mol. Biol."},{"key":"BFnsmb2555_CR10","doi-asserted-by":"publisher","first-page":"1054","DOI":"10.1111\/j.1365-2958.2008.06346.x","volume":"69","author":"T Kawahara","year":"2008","unstructured":"Kawahara, T. et al. Two essential MYST-family proteins display distinct roles in histone H4K10 acetylation and telomeric silencing in trypanosomes. Mol. Microbiol. 69, 1054\u20131068 (2008).","journal-title":"Mol. Microbiol."},{"key":"BFnsmb2555_CR11","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1128\/MMBR.64.2.435-459.2000","volume":"64","author":"DE Sterner","year":"2000","unstructured":"Sterner, D.E. & Berger, S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 64, 435\u2013459 (2000).","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"BFnsmb2555_CR12","doi-asserted-by":"publisher","first-page":"8807","DOI":"10.1073\/pnas.96.16.8807","volume":"96","author":"R Sternglanz","year":"1999","unstructured":"Sternglanz, R. & Schindelin, H. Structure and mechanism of action of the histone acetyltransferase Gcn5 and similarity to other N-acetyltransferases. Proc. Natl. Acad. Sci. USA 96, 8807\u20138808 (1999).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2555_CR13","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1016\/S1097-2765(00)00116-7","volume":"6","author":"Y Yan","year":"2000","unstructured":"Yan, Y., Barlev, N.A., Haley, R.H., Berger, S.L. & Marmorstein, R. Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases. Mol. Cell 6, 1195\u20131205 (2000).","journal-title":"Mol. Cell"},{"key":"BFnsmb2555_CR14","doi-asserted-by":"publisher","first-page":"862","DOI":"10.1038\/nsb0902-638","volume":"9","author":"Y Yan","year":"2002","unstructured":"Yan, Y., Harper, S., Speicher, D.W. & Marmorstein, R. The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Nat. Struct. Biol. 9, 862\u2013869 (2002).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsmb2555_CR15","doi-asserted-by":"publisher","first-page":"1209","DOI":"10.1534\/genetics.107.080135","volume":"178","author":"PV Decker","year":"2008","unstructured":"Decker, P.V., Yu, D.Y., Iizuka, M., Qiu, Q. & Smith, M.M. Catalytic-site mutations in the MYST family histone acetyltransferase Esa1. Genetics 178, 1209\u20131220 (2008).","journal-title":"Genetics"},{"key":"BFnsmb2555_CR16","doi-asserted-by":"publisher","first-page":"e32886","DOI":"10.1371\/journal.pone.0032886","volume":"7","author":"C Yang","year":"2012","unstructured":"Yang, C., Wu, J. & Zheng, Y.G. Function of the active site lysine autoacetylation in tip60 catalysis. PLoS ONE 7, e32886 (2012).","journal-title":"PLoS ONE"},{"key":"BFnsmb2555_CR17","doi-asserted-by":"publisher","first-page":"4153","DOI":"10.1093\/hmg\/ddp367","volume":"18","author":"Y Wang","year":"2009","unstructured":"Wang, Y. et al. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum. Mol. Genet. 18, 4153\u20134170 (2009).","journal-title":"Hum. Mol. Genet."},{"key":"BFnsmb2555_CR18","doi-asserted-by":"publisher","first-page":"15376","DOI":"10.1021\/bi026813c","volume":"41","author":"BI Giasson","year":"2002","unstructured":"Giasson, B.I. et al. The environmental toxin arsenite induces tau hyperphosphorylation. Biochemistry 41, 15376\u201315387 (2002).","journal-title":"Biochemistry"},{"key":"BFnsmb2555_CR19","doi-asserted-by":"publisher","first-page":"21517","DOI":"10.1073\/pnas.1013728107","volume":"107","author":"T Shida","year":"2010","unstructured":"Shida, T., Cueva, J.G., Xu, Z., Goodman, M.B. & Nachury, M.V. The major \u03b1-tubulin K40 acetyltransferase \u03b1TAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl. Acad. Sci. USA 107, 21517\u201321522 (2010).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2555_CR20","doi-asserted-by":"publisher","first-page":"297","DOI":"10.1016\/S0092-8674(00)80208-1","volume":"89","author":"G Drewes","year":"1997","unstructured":"Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.M. & Mandelkow, E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89, 297\u2013308 (1997).","journal-title":"Cell"},{"key":"BFnsmb2555_CR21","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1038\/nature09324","volume":"467","author":"JS Akella","year":"2010","unstructured":"Akella, J.S. et al. MEC-17 is an \u03b1-tubulin acetyltransferase. Nature 467, 218\u2013222 (2010).","journal-title":"Nature"},{"key":"BFnsmb2555_CR22","doi-asserted-by":"publisher","first-page":"834","DOI":"10.1126\/science.1175371","volume":"325","author":"C Choudhary","year":"2009","unstructured":"Choudhary, C. et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 325, 834\u2013840 (2009).","journal-title":"Science"},{"key":"BFnsmb2555_CR23","doi-asserted-by":"publisher","first-page":"13806","DOI":"10.1074\/jbc.M800247200","volume":"283","author":"EE Congdon","year":"2008","unstructured":"Congdon, E.E. et al. Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants. J. Biol. Chem. 283, 13806\u201313816 (2008).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2555_CR24","doi-asserted-by":"publisher","first-page":"197","DOI":"10.1016\/S1357-2725(97)00125-8","volume":"30","author":"FM Corrigan","year":"1998","unstructured":"Corrigan, F.M., Horrobin, D.F., Skinner, E.R., Besson, J.A. & Cooper, M.B. Abnormal content of n-6 and n-3 long-chain unsaturated fatty acids in the phosphoglycerides and cholesterol esters of parahippocampal cortex from Alzheimer's disease patients and its relationship to acetyl CoA content. Int. J. Biochem. Cell Biol. 30, 197\u2013207 (1998).","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"BFnsmb2555_CR25","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1038\/35012097","volume":"405","author":"H Kawasaki","year":"2000","unstructured":"Kawasaki, H. et al. ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. Nature 405, 195\u2013200 (2000).","journal-title":"Nature"},{"key":"BFnsmb2555_CR26","doi-asserted-by":"publisher","first-page":"4713","DOI":"10.1074\/jbc.M211811200","volume":"278","author":"C Lemercier","year":"2003","unstructured":"Lemercier, C. et al. Tip60 acetyltransferase activity is controlled by phosphorylation. J. Biol. Chem. 278, 4713\u20134718 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2555_CR27","doi-asserted-by":"publisher","first-page":"7679","DOI":"10.1074\/jbc.270.13.7679","volume":"270","author":"G Drewes","year":"1995","unstructured":"Drewes, G. et al. Microtubule-associated protein\/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J. Biol. Chem. 270, 7679\u20137688 (1995).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2555_CR28","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1016\/0197-4580(95)00025-A","volume":"16","author":"EM Mandelkow","year":"1995","unstructured":"Mandelkow, E.M. et al. Tau domains, phosphorylation, and interactions with microtubules. Neurobiol. Aging 16, 355\u2013362, discussion 362\u2013363 (1995).","journal-title":"Neurobiol. Aging"},{"key":"BFnsmb2555_CR29","doi-asserted-by":"publisher","first-page":"10047","DOI":"10.1021\/bi901090m","volume":"48","author":"D Fischer","year":"2009","unstructured":"Fischer, D. et al. Conformational changes specific for pseudophosphorylation at serine 262 selectively impair binding of tau to microtubules. Biochemistry 48, 10047\u201310055 (2009).","journal-title":"Biochemistry"},{"key":"BFnsmb2555_CR30","doi-asserted-by":"publisher","first-page":"a006247","DOI":"10.1101\/cshperspect.a006247","volume":"2","author":"EM Mandelkow","year":"2012","unstructured":"Mandelkow, E.M. & Mandelkow, E. Biochemistry and cell biology of tau protein in neurofibrillary degeneration. Cold Spring Harb. Perspect. Med. 2, a006247 (2012).","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"BFnsmb2555_CR31","doi-asserted-by":"publisher","first-page":"3549","DOI":"10.1021\/bi981874p","volume":"38","author":"A Schneider","year":"1999","unstructured":"Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E. & Mandelkow, E.M. Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 3549\u20133558 (1999).","journal-title":"Biochemistry"},{"key":"BFnsmb2555_CR32","doi-asserted-by":"publisher","first-page":"1241","DOI":"10.1038\/emboj.2011.471","volume":"31","author":"TJ Cohen","year":"2012","unstructured":"Cohen, T.J., Hwang, A.W., Unger, T., Trojanowski, J.Q. & Lee, V.M. Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J. 31, 1241\u20131252 (2012).","journal-title":"EMBO J."}],"container-title":["Nature Structural & Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2555.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2555","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2555.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T04:34:01Z","timestamp":1684470841000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb.2555"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,4,28]]},"references-count":32,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2013,6]]}},"alternative-id":["BFnsmb2555"],"URL":"https:\/\/doi.org\/10.1038\/nsmb.2555","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,4,28]]}}}