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PCGF Homologs, CBX Proteins, and RYBP Define Functionally Distinct PRC1 Family Complexes
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Summary The heterogeneous nature of mammalian PRC1 complexes has hindered our understanding of their biological functions. Here, we present a comprehensive proteomic and genomic analysis that uncovered six major groups of PRC1 complexes each containing a distinct PCGF subunit, a RING1A/B ubiquitin ligase, and a unique set of associated polypeptides. These PRC1 complexes differ in their genomic localization and only a small subset co-localize with H3K27me3. Further biochemical dissection revealed that the six PCGF-RING1A/B combinations form multiple complexes through association with RYBP or its homolog YAF2, which prevents the incorporation of other canonical PRC1 subunits such as CBX, PHC and SCM. Although both RYBP/YAF2- and CBX/PHC/SCM-containing complexes compact chromatin, only RYBP stimulates the activity of RING1B toward H2AK119ub1, suggesting a central role in PRC1 function. Knockdown of RYBP in ES cells compromised their ability to form embryoid bodies, likely because of defects in cell proliferation and maintenance of H2AK119ub1 level.
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Metadata
- Authors
- Gao, Z., Zhang, J., Bonasio, R., Strino, F., Sawai, A., Parisi, F., Kluger, Y., & Reinberg, D.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 45
- Issue
- 3
- Pages
- 344-356
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2025553576
- Cited by
- 848
- References
- 3
- FWCI
- 22.77
- Type
- journal article
- Language
- en
- Open access
- bronze
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