Reversible lysine acetylation of nuclear proteins such as histones is a long-established important regulatory mechanism for chromatin remodeling and transcription. In the cytoplasm, acetylation of a number of cytoskeletal proteins, including tubulin, cortactin, and the formin mDia2, regulates both cytoskeletal assembly and stability. More recently, acetylation of actin itself was revealed to regulate cytoplasmic actin polymerization through the formin INF2, with downstream effects on ER-to-mitochondrial calcium transfer, mitochondrial fission, and vesicle transport. This finding raises the possibility that actin acetylation, along with other post-translational modifications to actin, might constitute an “actin code,” similar to the “histone code” or “tubulin code,” controlling functional shifts to these central cellular proteins. Given the multiple roles of actin in nuclear functions, its modifications might also have important roles in gene expression.
Lysine acetylation of cytoskeletal proteins: Emergence of an actin code
M. A’s present address is Blavatnik Institute of Cell Biology, Dana Farber Cancer Institute, Harvard Medical School, Boston, MA.
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Mu A, Casey J. Latario, Laura E. Pickrell, Henry N. Higgs; Lysine acetylation of cytoskeletal proteins: Emergence of an actin code. J Cell Biol 7 December 2020; 219 (12): e202006151. doi: https://doi.org/10.1083/jcb.202006151
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