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

Authors: Belle, JI  Nijnik, A 
Citation: Belle JI and Nijnik A, Int J Biochem Cell Biol. 2014 May;50:161-74. doi: 10.1016/j.biocel.2014.03.004. Epub 2014 Mar 16.
Pubmed: (View Article at PubMed) PMID:24647359
DOI: Full-text: DOI:10.1016/j.biocel.2014.03.004

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.

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RGD Object Information
RGD ID: 9479061
Created: 2014-08-26
Species: All species
Last Modified: 2014-08-26
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.