ArticleThe EMBO journal1997
Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 147 citations in OpenAlex.
- cPRC1.2 and CTCF-mediated transition from poised to active chromatin loops at bivalent genes.EMBO reports · 2026Article
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- Structural basis of the histone ubiquitination read-write mechanism of RYBP-PRC1.Nature structural & molecular biology · 2024Article
- The Polycomb group geneFrontiers in neuroscience · 2022Article
- Dynamics of H3K27me3 Modification on Plant Adaptation to Environmental Cues.Plants (Basel, Switzerland) · 2021Review
- SUMOylated PRC1 controls histone H3.3 deposition and genome integrity of embryonic heterochromatin.The EMBO journal · 2020Article
- Mammalian CBX7 isoforms p36 and p22 exhibit differential responses to serum, varying functions for proliferation, and distinct subcellular localization.Scientific reports · 2020Article
- The CBX family of proteins in transcriptional repression and memory.Journal of biosciences · 2020Article
- Requirement for PRC1 subunit BMI1 in host gene activation by Epstein-Barr virus protein EBNA3C.Nucleic acids research · 2019Article
- Nuclear condensates of the Polycomb protein chromobox 2 (CBX2) assemble through phase separation.The Journal of biological chemistry · 2019Article
- Epigenetic Targets in Synovial Sarcoma: A Mini-Review.Frontiers in oncology · 2019Review
- Mutation of a nucleosome compaction region disrupts Polycomb-mediated axial patterning.Science (New York, N.Y.) · 2017Article
- Polycomb inhibits histone acetylation by CBP by binding directly to its catalytic domain.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Arginine Methyltransferase PRMT6 Cooperates with Polycomb Proteins in Regulating HOXA Gene Expression.PloS one · 2016Article
- Regulation of gene transcription by Polycomb proteins.Science advances · 2015Article
- Transcriptional repression by PRC1 in the absence of H2A monoubiquitylation.Genes & development · 2015Article
- Cbx2 stably associates with mitotic chromosomes via a PRC2- or PRC1-independent mechanism and is needed for recruiting PRC1 complex to mitotic chromosomes.Molecular biology of the cell · 2014Article
- Article
- Mitogen-activated protein kinase signaling mediates phosphorylation of polycomb ortholog Cbx7.The Journal of biological chemistry · 2013Article
- Ring1b bookmarks genes in pancreatic embryonic progenitors for repression in adult β cells.Genes & development · 2013Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Drosophila, the products of the Polycomb group (Pc-G) of genes act as chromatin-associated multimeric protein complexes that repress expression of homeotic genes. Vertebrate Pc-G homologues have been identified, but the nature of the complexes they form and the mechanisms of their action are largely unknown. The Polycomb homologue M33 is implicated in mesoderm patterning in the mouse and here we show that it acts as a transcriptional repressor in transiently transfected cells. Furthermore, we have identified two murine proteins, Ring1A and Ring1B, that interact directly with the repressor domain of M33. Ring1A and Ring1B display blocks of similarity throughout their sequences, including an N-terminal RING finger domain. However, the interaction with M33 occurs through a region at the C-terminus. Ring1A represses transcription through sequences not involved in M33 binding. Ring1A protein co-localizes in nuclear domains with M33 and other Pc-G homologues, such as Bmi1. The expression of Ring1A at early stages of development is restricted to the neural tube, whereas M33 is expressed ubiquitously. Within the neural tube, Ring1A RNA is located at the rhombomere boundaries of the hindbrain. Taken together, these data suggest that Ring1A may contribute to a tissue-specific function of Pc-G-protein complexes during mammalian development.
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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.