BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling

The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair foci, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologous recombination by...

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Detalles Bibliográficos
Autor principal: Rabl, Julius
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692841/
https://www.ncbi.nlm.nih.gov/pubmed/33142801
http://dx.doi.org/10.3390/biom10111503
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author Rabl, Julius
author_facet Rabl, Julius
author_sort Rabl, Julius
collection PubMed
description The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair foci, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologous recombination by limiting resection. BRISC forms a complex with metabolic enzyme SHMT2 and regulates the immune response, mitosis, and hematopoiesis. Almost two decades of research have revealed how BRCA1-A and BRISC use the same core of subunits to perform very distinct biological tasks.
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spelling pubmed-76928412020-11-28 BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling Rabl, Julius Biomolecules Review The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair foci, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologous recombination by limiting resection. BRISC forms a complex with metabolic enzyme SHMT2 and regulates the immune response, mitosis, and hematopoiesis. Almost two decades of research have revealed how BRCA1-A and BRISC use the same core of subunits to perform very distinct biological tasks. MDPI 2020-10-31 /pmc/articles/PMC7692841/ /pubmed/33142801 http://dx.doi.org/10.3390/biom10111503 Text en © 2020 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Rabl, Julius
BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title_full BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title_fullStr BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title_full_unstemmed BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title_short BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
title_sort brca1-a and brisc: multifunctional molecular machines for ubiquitin signaling
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7692841/
https://www.ncbi.nlm.nih.gov/pubmed/33142801
http://dx.doi.org/10.3390/biom10111503
work_keys_str_mv AT rabljulius brca1aandbriscmultifunctionalmolecularmachinesforubiquitinsignaling

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