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Deubiquitinase USP2 stabilizes the MRE11-RAD50-NBS1 complex at DNA double-strand break sites by counteracting the ubiquitination of NBS1.


ABSTRACT:

SUBMITTER: Kim H 

PROVIDER: S-EPMC9758435 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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Deubiquitinase USP2 stabilizes the MRE11-RAD50-NBS1 complex at DNA double-strand break sites by counteracting the ubiquitination of NBS1.

Kim Hyunsup H   Kim Dongmin D   Choi Hyemin H   Shin Gwangsu G   Lee Joon-Kyu JK  

The Journal of biological chemistry 20221125 1


The MRE11-RAD50-NBS1 (MRN) complex plays essential roles in the cellular response to DNA double-strand breaks (DSBs), which are the most cytotoxic DNA lesions, and is a target of various modifications and controls. Recently, lysine 48-linked ubiquitination of NBS1, resulting in premature disassembly of the MRN complex from DSB sites, was observed in cells lacking RECQL4 helicase activity. However, the role and control of this ubiquitination during the DSB response in cells with intact RECQL4 rem  ...[more]

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