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.
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Nature Portfolio
2018
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oai:doaj.org-article:1e3a338b35724ff5b4dbc88530cac69f2021-12-02T16:56:37ZUSP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A10.1038/s41467-017-02653-32041-1723https://doaj.org/article/1e3a338b35724ff5b4dbc88530cac69f2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02653-3https://doaj.org/toc/2041-1723BRCA1 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.Michael UckelmannRuth M. DenshamRoy BaasHerrie H. K. WinterwerpAlexander FishTitia K. SixmaJoanna R. MorrisNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-16 (2018) |
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Science Q |
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Science Q 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 |
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. |
format |
article |
author |
Michael Uckelmann Ruth M. Densham Roy Baas Herrie H. K. Winterwerp Alexander Fish Titia K. Sixma Joanna R. Morris |
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 Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/1e3a338b35724ff5b4dbc88530cac69f |
work_keys_str_mv |
AT michaeluckelmann usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT ruthmdensham usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT roybaas usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT herriehkwinterwerp usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT alexanderfish usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT titiaksixma usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a AT joannarmorris usp48restrainsresectionbysitespecificcleavageofthebrca1ubiquitinmarkfromh2a |
_version_ |
1718382785506312192 |