When the RAP (80) fades out, you can hear BRCA1 RING.

BRCA1 Protein / genetics Carrier Proteins / metabolism DNA-Binding Proteins / metabolism Histone Chaperones / metabolism Nuclear Proteins / metabolism Ubiquitin-Protein Ligases / genetics

Journal

EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049

Informations de publication

Date de publication:
06 12 2021
Historique:
received: 07 10 2021
accepted: 13 10 2021
pubmed: 3 11 2021
medline: 15 3 2022
entrez: 2 11 2021
Statut: ppublish

Résumé

The tumor suppressor protein BRCA1 plays an important role in DNA repair by homologous recombination. Despite being encoded by the first familial breast and ovarian cancer gene identified, how BRCA1 is recruited to sites of DNA damage to execute its repair functions has remained poorly understood. Several recent studies highlight the role of its constitutive interaction partner BARD1 in this process. In this issue, parallel work by Sherker et al (2021) focused on a second route of BRCA1 recruitment, connected to the BRCA1-A complex protein RAP80. Studying BRCA1 recruitment in RAP80-deficient cells exposed a critical role for the BRCA1 RING domain and its associated ubiquitin ligase activity. Given that tumors expressing RING-less BRCA1 isoforms can become resistant to therapy, targeting the RAP80 recruitment axis in such tumors might restore effective treatment.

Identifiants

DOI: 10.15252/embr.202154116 PMID: 34726332 PMC: PMC8647006
pubmed: 34726332
doi: 10.15252/embr.202154116
pmc: PMC8647006
doi:

Substances chimiques

BRCA1 Protein 0
Carrier Proteins 0
DNA-Binding Proteins 0
Histone Chaperones 0
Nuclear Proteins 0
Ubiquitin-Protein Ligases EC 2.3.2.27

Types de publication

Journal Article Comment

Langues

eng

Sous-ensembles de citation

IM

Pagination

e54116

Commentaires et corrections

Type : CommentOn

Informations de copyright

© 2021 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

Références

Mol Cell. 2021 Jul 1;81(13):2765-2777.e6
pubmed: 34102105
EMBO Rep. 2021 Dec 6;22(12):e53679
pubmed: 34726323
Nature. 2021 Aug;596(7872):433-437
pubmed: 34321663
EMBO Rep. 2021 Dec 6;22(12):e54116
pubmed: 34726332
Nat Struct Mol Biol. 2021 Mar;28(3):268-277
pubmed: 33589814
Life Sci Alliance. 2021 Apr 2;4(6):
pubmed: 33811064
Nature. 2021 Aug;596(7872):438-443
pubmed: 34321665
Nat Cell Biol. 2019 Mar;21(3):311-318
pubmed: 30804502
Nat Struct Mol Biol. 2016 Jul;23(7):647-55
pubmed: 27239795
Nat Commun. 2021 Aug 18;12(1):5016
pubmed: 34408138
Nat Rev Mol Cell Biol. 2020 May;21(5):284-299
pubmed: 32094664

Auteurs

Andreas Panagopoulos (A)

Department of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
ORCID: 0000-0002-7787-6938

Matthias Altmeyer (M)

Department of Molecular Mechanisms of Disease, University of Zurich, Zurich, Switzerland.
ORCID: 0000-0003-3780-1170

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Facteurs de transcription › Protéine BRCA1 › When the RAP (80) fades out, you can hear BRCA1 RING.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › When the RAP (80) fades out, you can hear BRCA1 RING.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de liaison à l'ADN › When the RAP (80) fades out, you can hear BRCA1 RING.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Chaperons moléculaires › Chaperons d'histones › When the RAP (80) fades out, you can hear BRCA1 RING.
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines nucléaires › When the RAP (80) fades out, you can hear BRCA1 RING.
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Ubiquitin-protein ligase complexes › Ubiquitin-protein ligases › When the RAP (80) fades out, you can hear BRCA1 RING.