Journal
EMBO JOURNAL
Volume 29, Issue 15, Pages 2553-2565Publisher
WILEY
DOI: 10.1038/emboj.2010.129
Keywords
chromatin; INK4a; Polycomb; transcription; ubiquitination
Categories
Funding
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BBS/E/B/0000L748, BBS/E/B/0000H234] Funding Source: researchfish
- BBSRC [BBS/E/B/0000H234, BBS/E/B/0000L748] Funding Source: UKRI
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An important facet of transcriptional repression by Polycomb repressive complex 1 (PRC1) is the mono-ubiquitination of histone H2A by the combined action of the Posterior sex combs (Psc) and Sex combs extra (Sce) proteins. Here, we report that two ubiquitin-specific proteases, USP7 and USP11, co-purify with human PRC1-type complexes through direct interactions with the Psc orthologues MEL18 and BMI1, and with other PRC1 components. Ablation of either USP7 or USP11 in primary human fibroblasts results in de-repression of the INK4a tumour suppressor accompanied by loss of PRC1 binding at the locus and a senescence-like proliferative arrest. Mechanistically, USP7 and USP11 regulate the ubiquitination status of the Psc and Sce proteins themselves, thereby affecting their turnover and abundance. Our results point to a novel function for USPs in the regulation and function of Polycomb complexes. The EMBO Journal (2010) 29, 2553-2565. doi:10.1038/emboj.2010.129; Published online 2 July 2010
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