ArticleNature communications2015
BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 136 citations in OpenAlex.
- Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1.Nature structural & molecular biology · 2026Article
- cPRC1.2 and CTCF-mediated transition from poised to active chromatin loops at bivalent genes.EMBO reports · 2026Article
- Hydrophobic Tag Degraders Overcome Endocrine-Resistant Breast Cancer by Recruiting HSP27-Mediated E3 Ligase Complex for ERα Proteasomal Degradation.Angewandte Chemie (International ed. in English) · 2026Article
- Rare protein-coding variation and the genetic architecture of height in >1.4 million individuals.medRxiv : the preprint server for health sciences · 2026Article
- Sustained PRC1.1 activity preserves gene repression independently of PRC2.2 and restrains leukemic cell differentiation.Nucleic acids research · 2026Article
- Phosphorylated ubiquitin is a secondary messenger and an epigenetic mark mediating mitochondria to nucleus signaling.bioRxiv : the preprint server for biology · 2026Article
- Polycomb-mediated 3D chromatin interactions in gene regulation.Current opinion in genetics & development · 2026Review
- Chromatin folding by the Polycomb group proteins and its elusive role in epigenetic repression.The FEBS journal · 2026Review
- Homology search confirms widespread presence of BBSome proteins in Hexapoda with implications for potential non-ciliary BBS protein functions in honey bees.Scientific reports · 2025Article
- Distinct specificity and functions of PRC2 subcomplexes in human stem cells and cardiac differentiation.Molecular cell · 2025Article
- BMI1 regulates human erythroid self-renewal through both gene repression and gene activation.Nature communications · 2025Article
- Noncanonical PRC1.1 targets BTG2 to retain cyclin gene expression and cell growth in neuroblastoma.Oncogenesis · 2025Article
- Single-molecule analysis reveals the mechanism of chromatin ubiquitylation by variant PRC1 complexes.Science advances · 2025Article
- A conserved switch to less catalytically active Polycomb repressive complexes in non-dividing cells.Cell reports · 2025Article
- Article
- Nuclear PCGF3 inhibits the antiviral immune response by suppressing the interferon-stimulated gene.Cell death discovery · 2024Article
- PRC1 Protein Subcomplexes Architecture: Focus on the Interplay between Distinct PCGF Subunits in Protein Interaction Networks.International journal of molecular sciences · 2024Article
- Calcium modulates the tethering of BCOR-PRC1.1 enzymatic core to KDM2B via liquid-liquid phase separation.Communications biology · 2024Article
- Degraders in epigenetic therapy: PROTACs and beyond.Theranostics · 2024Review
- DNA elements tether canonical Polycomb Repressive Complex 1 to human genes.Nucleic acids research · 2023Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polycomb repressive complex 1 (PRC1) is required for ubiquitination of histone H2A lysine 119, an epigenetic mark associated with repression of genes important in developmental regulation. The E3 ligase activity of PRC1 resides in the RING1A/B subunit when paired with one of six PCGF partners. The best known of these is the oncogene BMI1/PCGF4. We find that canonical PRC1 E3 ligases such as PCGF4-RING1B have intrinsically very low enzymatic activity compared with non-canonical PRC1 RING dimers. The structure of a high-activity variant in complex with E2 (PCGF5-RING1B-UbcH5c) reveals only subtle differences from an earlier PCGF4 complex structure. However, two charged residues present in the modelled interface with E2-conjugated ubiquitin prove critical: in BMI1/PCGF4, these residues form a salt bridge that may limit efficient ubiquitin transfer. The intrinsically low activity of the PCGF4-RING1B heterodimer is offset by a relatively favourable interaction with nucleosome substrates, resulting in an efficient site-specific monoubiquitination.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.