Dynamic phosphorylation of Histone Deacetylase 1 by Aurora kinases during mitosis regulates zebrafish embryos development

• Published in: Scientific reports 2016-07, Vol.6 (1), p.30213-30213, Article 30213
• Main Authors: Loponte, Sara, Segré, Chiara V., Senese, Silvia, Miccolo, Claudia, Santaguida, Stefano, Deflorian, Gianluca, Citro, Simona, Mattoscio, Domenico, Pisati, Federica, Moser, Mirjam A., Visintin, Rosella, Seiser, Christian, Chiocca, Susanna
• Format: Article
• Language: English
• Subjects: 13/106; 13/109; 13/31; 13/51; 14/19; 38; 38/15; 38/70; 38/77; 38/89; 38/90; 42; 631/136/2091; 631/80/458/1733; 64; Humanities and Social Sciences; multidisciplinary; Science; Science (multidisciplinary)
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep30213

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.