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• W2476030183 abstract "Histone deacetylases (HDACs) catalyze the removal of acetyl molecules from histone and non-histone substrates playing important roles in chromatin remodeling and control of gene expression. Class I HDAC1 is a critical regulator of cell cycle progression, cellular proliferation and differentiation during development; it is also regulated by many post-translational modifications (PTMs). Herein we characterize a new mitosis-specific phosphorylation of HDAC1 driven by Aurora kinases A and B. We show that this phosphorylation affects HDAC1 enzymatic activity and it is critical for the maintenance of a proper proliferative and developmental plan in a complex organism. Notably, we find that Aurora-dependent phosphorylation of HDAC1 regulates histone acetylation by modulating the expression of genes directly involved in the developing zebrafish central nervous system. Our data represent a step towards the comprehension of HDAC1 regulation by its PTM code, with important implications in unravelling its roles both in physiology and pathology." @default.
• W2476030183 created "2016-08-23" @default.
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• W2476030183 date "2016-07-01" @default.
• W2476030183 modified "2023-10-12" @default.
• W2476030183 title "Dynamic phosphorylation of Histone Deacetylase 1 by Aurora kinases during mitosis regulates zebrafish embryos development" @default.
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• W2476030183 doi "https://doi.org/10.1038/srep30213" @default.
• W2476030183 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4960611" @default.
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