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SENP3 and USP7 regulate Polycomb-rixosome interactions and silencing functions(ChIP-seq)

ABSTRACT: SENP3 and USP7 regulate Polycomb-rixosome interactions and silencing functions(ChIP-seq)

PROVIDER: PRJNA808419 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18074955.fastq.gz	Fastqsanger.gz
	SRR18074956.fastq.gz	Fastqsanger.gz
	SRR18074957.fastq.gz	Fastqsanger.gz
	SRR18074958.fastq.gz	Fastqsanger.gz
	SRR18074959.fastq.gz	Fastqsanger.gz

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Project description:Ubiquitin-specific protease 7 (USP7) has been implicated in cancer progression and neurodevelopment. However, its molecular targets remain poorly characterized. We combined quantitative proteomics, transcriptomics, and epigenomics to define the core USP7 network. Our multi-omics analysis reveals USP7 as a control hub that links genome regulation, tumor suppression, and histone H2A ubiquitylation (H2AK119ub1) by noncanonical Polycomb-repressive complexes (ncPRC1s). USP7 strongly stabilizes ncPRC1.6 and, to a lesser extent, ncPRC1.1. Moreover, USP7 represses expression of AUTS2, which suppresses H2A ubiquitylation by ncPRC1.3/5. Collectively, these USP7 activities promote the genomic deposition of H2AK119ub1 by ncPRC1, especially at transcriptionally repressed loci. Notably, USP7-dependent changes in H2AK119ub1 levels are uncoupled from H3K27me3. Even complete loss of the PRC1 catalytic core and H2AK119ub1 has only a limited effect on H3K27me3. Besides defining the USP7 regulome, our results reveal that H2AK119ub1 dosage is largely disconnected from H3K27me3.

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