Polycomb complex protein: Difference between revisions
No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| (9 intermediate revisions by 3 users not shown) | |||
| Line 1: | Line 1: | ||
<StructureSection load='' size='350' side='right' caption='Structure of a Bmi1 protein' scene='78/787701/Bmi1_isolada_da_2h0d/3'> | <StructureSection load='' size='350' side='right' caption='Structure of a Bmi1 protein complex with ubiquitin ligase protein RING2 (PDB id [[2h0d]])' scene='78/787701/Bmi1_isolada_da_2h0d/3'> | ||
== Function == | |||
'''Polycomb group ring finger protein 1''' (Pcgf1) is a link between Polycomb function and pluripotency <ref>PMID:26687479</ref>.<br /> | |||
'''Polycomb group ring finger protein 4''' (Pcgf4) or (BMI1) see below <ref>PMID:23523425</ref>.<br /> | |||
'''Polycomb group ring finger protein 5''' (Pcgf5) is regulator of gene expression and development <ref>PMID:29765032</ref>.<br /> | |||
'''Polycomb group ring finger protein 6''' (Pcgf6) has a role in safeguarding lineage decisions and in preventing aberrant expression of germ cell-related gens <ref>PMID:32482889</ref>.<br /> | |||
B-cell-specific Moloney leukemia virus insertion site 1 (BMI1) is a ring finger protein that is component of a <scene name='78/787701/2h0d/2'>Polycomb group (PcG) multiprotein PRC1 complex</scene>, which epigenetically repress regulatory genes related to embryonic development and self-renewal of somatic stem-cells. The name come from the original identification of BMI1 as an oncogene cooperating with a myc gene in lymphomagenesis <ref>DOI: 10.1038/16476</ref> . It became clear that the Bmi1 protein is part of an E3 ubiquitin ligase complex (PRC1) <ref>DOI: 10.1038/nature02985</ref> and that this complex has an important role in gene regulation during development. | '''B-cell-specific Moloney leukemia virus insertion site 1''' (BMI1) is a ring finger protein that is component of a <scene name='78/787701/2h0d/2'>Polycomb group (PcG) multiprotein PRC1 complex</scene>, which epigenetically repress regulatory genes related to embryonic development and self-renewal of somatic stem-cells. The name come from the original identification of BMI1 as an oncogene cooperating with a myc gene in lymphomagenesis <ref>DOI: 10.1038/16476</ref> . It became clear that the Bmi1 protein is part of an E3 ubiquitin ligase complex (PRC1) <ref>DOI: 10.1038/nature02985</ref> and that this complex has an important role in gene regulation during development. | ||
Monoubiquitinated H2A is enriched on the inactive human female X-chromosome. The inactivation of one of the X-chromosome is responsible for “dosing” the X-chromosome expression, which leads to the physiological X expression levels in females similar to the X expression levels in males (which has only one X). | Monoubiquitinated H2A is enriched on the inactive human female X-chromosome. The inactivation of one of the X-chromosome is responsible for “dosing” the X-chromosome expression, which leads to the physiological X expression levels in females similar to the X expression levels in males (which has only one X). | ||
| Line 11: | Line 15: | ||
PcG PRC1 is responsible for chromatin remodeling and histone modification, mediating monoubiquitination of histone H2A at Lysine 119, rendering chromatin heritably changed in its expressibility. BMI1 regulates the E3 ubiquitin-protein ligase activity of RING1b, which is also a protein component of the PcG PRC1 complex. | PcG PRC1 is responsible for chromatin remodeling and histone modification, mediating monoubiquitination of histone H2A at Lysine 119, rendering chromatin heritably changed in its expressibility. BMI1 regulates the E3 ubiquitin-protein ligase activity of RING1b, which is also a protein component of the PcG PRC1 complex. | ||
== Structure == | == Structure == | ||
| Line 56: | Line 59: | ||
Proposed architecture of the PRC1 complex oligomer. | Proposed architecture of the PRC1 complex oligomer. | ||
== Disease == | == Disease == | ||
| Line 71: | Line 72: | ||
BMI1 also inhibits the CDKN1A gene, an important inhibitor of the cellular cycle, promoting the cellular proliferation. The inhibition of CDKN1A gene is promoted when a lncRNA, FALEC (focally amplified long non-coding RNA on chromosome 1 gene), stabilizes BMI1. | BMI1 also inhibits the CDKN1A gene, an important inhibitor of the cellular cycle, promoting the cellular proliferation. The inhibition of CDKN1A gene is promoted when a lncRNA, FALEC (focally amplified long non-coding RNA on chromosome 1 gene), stabilizes BMI1. | ||
== Conservation == | == Conservation == | ||
| Line 98: | Line 97: | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
==Polycomb complex protein 3D structures== | |||
[[Polycomb complex proteins 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
== External resources== | == External resources== | ||
| Line 111: | Line 107: | ||
*[http://www.uniprot.org/uniprot/P35226#structure Aggregated information about BMI1 protein in UniProt database] | *[http://www.uniprot.org/uniprot/P35226#structure Aggregated information about BMI1 protein in UniProt database] | ||
*[https://www.genecards.org/cgi-bin/carddisp.pl?gene=BMI1 Aggregated information about BMI1 gene in GeneCards database] | *[https://www.genecards.org/cgi-bin/carddisp.pl?gene=BMI1 Aggregated information about BMI1 gene in GeneCards database] | ||
</StructureSection> | |||
[[Category:Topic Page]] | |||