期刊
BIOCHEMICAL JOURNAL
卷 473, 期 -, 页码 1859-1868出版社
PORTLAND PRESS LTD
DOI: 10.1042/BCJ20160172
关键词
alpha TAT1; HDAC6; lysine 40; non-canonical tubulin acetylation
资金
- Institut National Du Cancer [INCa] [2013-82]
- Fondation Recherche Medicale [FRM] [DBI20141231321, DEI20151234416]
- Agence Nationale de la Recherche [ANR] [EpiSperm3]
- Universite Grenoble Alpes [UGA] [AGIR-POLE FRAG15CS08]
Tubulin heterodimers are the building block of microtubules, which are major elements of the cytoskeleton. Several types of post-translational modifications are found on tubulin subunits as well as on the microtubule polymer to regulate the multiple roles of microtubules. Acetylation of lysine 40 (K40) of the alpha-tubulin subunit is one of these post-translational modifications which has been extensively studied. We summarize the current knowledge about the structural aspects of K40 acetylation, the functional consequences, the enzymes involved and their regulation. Most importantly, we discuss the potential importance of the recently discovered additional acetylation acceptor lysines in tubulin subunits and highlight the urgent need to study tubulin acetylation in a more integrated perspective.
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