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Int J Biochem Cell Biol. 2014 May;50:161-74. doi: 10.1016/j.biocel.2014.03.004. Epub 2014 Mar 16.

H2A-DUBbing the mammalian epigenome: expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology.

Author information

1
Department of Physiology, McGill University, Canada; Complex Traits Group, McGill University, Canada.
2
Department of Physiology, McGill University, Canada; Complex Traits Group, McGill University, Canada. Electronic address: anastasiya.nyzhnyk@mcgill.ca.

Abstract

Posttranslational modifications of histone H2A through the attachment of ubiquitin or poly-ubiquitin conjugates are common in mammalian genomes and play an important role in the regulation of chromatin structure, gene expression, and DNA repair. Histone H2A deubiquitinases (H2A-DUBs) are a group of structurally diverse enzymes that catalyze the removal ubiquitin from histone H2A. In this review we provide a concise summary of the mechanisms that mediate histone H2A ubiquitination in mammalian cells, and review our current knowledge of mammalian H2A-DUBs, their biochemical activities, and recent developments in our understanding of their functions in mammalian physiology.

KEYWORDS:

Chromatin; DNA repair; Deubiquitinase; Histone H2A; Transcriptional regulation

PMID:
24647359
DOI:
10.1016/j.biocel.2014.03.004
[Indexed for MEDLINE]

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