ZFIN ID: ZDB-PUB-160728-14
Dynamic phosphorylation of Histone Deacetylase 1 by Aurora kinases during mitosis regulates zebrafish embryos development
Loponte, S., Segré, C.V., Senese, S., Miccolo, C., Santaguida, S., Deflorian, G., Citro, S., Mattoscio, D., Pisati, F., Moser, M.A., Visintin, R., Seiser, C., Chiocca, S.
Date: 2016
Source: Scientific Reports   6: 30213 (Journal)
Registered Authors: Deflorian, Gianluca
Keywords: Cell proliferation, Phosphorylation
MeSH Terms:
  • Acetylation
  • Animals
  • Aurora Kinases/metabolism*
  • Embryonic Development*
  • Genes, Regulator
  • Histone Deacetylase 1/metabolism*
  • Histones/metabolism
  • Mitosis*
  • Phosphorylation
  • Zebrafish/embryology*
PubMed: 27458029 Full text @ Sci. Rep.
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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.
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