ArticleBiochemistry2020
Structure and Role of BCOR PUFD in Noncanonical PRC1 Assembly and Disease.
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Sustained PRC1.1 activity preserves gene repression independently of PRC2.2 and restrains leukemic cell differentiation.Nucleic acids research · 2026Article
- Analysis of a BCOR internal tandem duplication in mouse embryonic stem cell to neuronal precursor differentiation.Genetics · 2025Article
- Calcium modulates the tethering of BCOR-PRC1.1 enzymatic core to KDM2B via liquid-liquid phase separation.Communications biology · 2024Article
- Acute monocytic leukemia with KMT2A::LASP1 developed 9 months after diagnosis of acute megakaryoblastic leukemia in a 2-year-old boy.International journal of hematology · 2023Article
- Differential diagnosis of uterine adenosarcoma: identification of JAZF1-BCORL1 rearrangement by comprehensive cancer genomic profiling.Diagnostic pathology · 2023Article
- BCOR gene alterations in hematologic diseases.Blood · 2021Review
- Clinicopathological and genomic characterization of BCORL1-driven high-grade endometrial stromal sarcomas.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2021Article
- LG-ESSs and HG-ESSs: underlying molecular alterations and potential therapeutic strategies.Journal of Zhejiang University. Science. B · 2021Review
- Isocitrate Dehydrogenase-Mutant WHO Grade 4 Astrocytoma with BCOR Alteration: Case Report.Case reports in oncologyArticle
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Polycomb repression complex 1 (PRC1) is a multiprotein assembly that regulates transcription. The Polycomb group ring finger 1 protein (PCGF1) is central in the assembly of the noncanonical PRC1 variant called PRC1.1 through its direct interaction with BCOR (BCL-6-interacting corepressor) or its paralog, BCOR-like 1 (BCORL1). Previous structural studies revealed that the C-terminal PUFD domain of BCORL1 is necessary and sufficient to heterodimerize with the RAWUL domain of PCGF1 and, together, form a new protein-protein binding interface that associates with the histone demethylase KDM2B. Here, we show that the PUFD of BCOR and BCORL1 differ in their abilities to assemble with KDM2B. Unlike BCORL1, the PUFD of BCOR alone does not stably assemble with KDM2B. Rather, additional residues N-terminal to the BCOR PUFD are necessary for stable association. Nuclear magnetic resonance (NMR) structure determination and
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Registered trials
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.