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
Description
Summary: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.
ISSN:2041-1723

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