title: H2A-DUBbing the mammalian epigenome: expanding frontiers for histone H2A deubiquitinating enzymes in cell biology and physiology.
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.
authors.affiliation: Department of Physiology, McGill University, Canada; Complex Traits Group, McGill University, Canada.
authors.forename: Jad I
authors.initials: JI
authors.lastname: Belle
authors.affiliation: Department of Physiology, McGill University, Canada; Complex Traits Group, McGill University, Canada. Electronic address: anastasiya.nyzhnyk@mcgill.ca.
authors.forename: Anastasia
authors.initials: A
authors.lastname: Nijnik
mesh_terms: D000818:Animals; D004260:DNA Repair; D057890:Epigenomics; D006657:Histones / Q000378:metabolism*; D006801:Humans; D011499:Protein Processing, Post-Translational; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*; D064570:Ubiquitin-Specific Proteases / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D006657:Histones; D044767:Ubiquitin-Protein Ligases; D064570:Ubiquitin-Specific Proteases
keywords: Chromatin; DNA repair; Deubiquitinase; Histone H2A; Transcriptional regulation