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The ubiquitin E3/E4 ligase UBE4A adjusts protein ubiquitylation and accumulation at sites of DNA damage, facilitating double-strand break repair

AuthorsBaranes-Bachar, Keren; Levy-Barda, Adva; Oehler, Judith; Reid, Dylan A.; Soria-Bretones, Isabel; Voss, Ty C.; Chung, Dudley; Park, Yoon; Liu, Chao; Yoon, Jong-Bok; Li, Wei; Dellaire, Graham; Misteli, Tom; Huertas Sánchez, Pablo CSIC ORCID; Rothenberg, Eli; Ramadan, Kristijan; Ziv, Yael; Shiloh, Yosef
KeywordsGenome stability
DNA damage
Double-strand breaks
Issue Date1-Mar-2018
CitationMolecular Cell 69(5): 866-878.e7 (2018)
AbstractDouble-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning: the E3/E4 ubiquitin ligase UBE4A. UBE4A’s recruitment to sites of DNA damage is dependent on primary E3 ligases in the DDR and promotes enhancement and sustainment of K48- and K63-linked ubiquitin chains at these sites. This step is required for timely recruitment of the RAP80 and BRCA1 proteins and proper organization of RAP80- and BRCA1-associated protein complexes at DSB sites. This pathway is essential for optimal end resection at DSBs, and its abrogation leads to upregulation of the highly mutagenic alternative end-joining repair at the expense of error-free homologous recombination repair. Our data uncover a critical regulatory level in the DSB response and underscore the importance of fine-tuning the complex DDR network for accurate and balanced execution of DSB repair.
Publisher version (URL)https://doi.org/10.1016/j.molcel.2018.02.002
Appears in Collections:(CABIMER) Artículos
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