USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A

USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A

BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.

Bibliographic Details
Main Authors: Michael Uckelmann, Ruth M. Densham, Roy Baas, Herrie H. K. Winterwerp, Alexander Fish, Titia K. Sixma, Joanna R. Morris
Format: Article
Language:English
Published: Nature Publishing Group 2018-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-02653-3
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spelling doaj-1e3a338b35724ff5b4dbc88530cac69f2021-05-11T09:34:14ZengNature Publishing GroupNature Communications2041-17232018-01-019111610.1038/s41467-017-02653-3USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2AMichael Uckelmann0Ruth M. Densham1Roy Baas2Herrie H. K. Winterwerp3Alexander Fish4Titia K. Sixma5Joanna R. Morris6Division of Biochemistry and Cancer Genomics Centre, Netherlands Cancer InstituteBirmingham Centre for Genome Biology and Institute of Cancer and Genomic Sciences, Medical and Dental Schools, University of BirminghamDivision of Biochemistry and Cancer Genomics Centre, Netherlands Cancer InstituteDivision of Biochemistry and Cancer Genomics Centre, Netherlands Cancer InstituteDivision of Biochemistry and Cancer Genomics Centre, Netherlands Cancer InstituteDivision of Biochemistry and Cancer Genomics Centre, Netherlands Cancer InstituteBirmingham Centre for Genome Biology and Institute of Cancer and Genomic Sciences, Medical and Dental Schools, University of BirminghamBRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.https://doi.org/10.1038/s41467-017-02653-3
collection DOAJ
language English
format Article
sources DOAJ
author Michael Uckelmann
Ruth M. Densham
Roy Baas
Herrie H. K. Winterwerp
Alexander Fish
Titia K. Sixma
Joanna R. Morris
spellingShingle Michael Uckelmann
Ruth M. Densham
Roy Baas
Herrie H. K. Winterwerp
Alexander Fish
Titia K. Sixma
Joanna R. Morris
USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
Nature Communications
author_facet Michael Uckelmann
Ruth M. Densham
Roy Baas
Herrie H. K. Winterwerp
Alexander Fish
Titia K. Sixma
Joanna R. Morris
author_sort Michael Uckelmann
title USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
title_short USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
title_full USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
title_fullStr USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
title_full_unstemmed USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
title_sort usp48 restrains resection by site-specific cleavage of the brca1 ubiquitin mark from h2a
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-01-01
description BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.
url https://doi.org/10.1038/s41467-017-02653-3
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