Mixed ubiquitin chains regulate DNA repair
- Gergely Rona1,2 and
- Michele Pagano1,2,3
- 1Department of Biochemistry and Molecular Pharmacology;
- 2Perlmutter Cancer Center;
- 3Howard Hughes Medical Institute, New York University School of Medicine, New York, New York 10016, USA
- Corresponding author: michele.pagano{at}nyulangone.org
Abstract
Diverse linkage in polyubiquitin chain structure gives cells an unparalleled complexity to virtually modulate all aspects of cell biology. Substrates can be covalently modified by ubiquitin chains of different topology. Proper DNA damage response takes advantage of this regulatory system and heavily relies on ubiquitin-based signaling. Moreover, increasing evidence suggests that chain specificity dictates DNA repair outcome. In this issue of Genes & Development, Wu and colleagues (pp. 1702–1717) show that Cezanne and Cezanne2, two paralogous deubiquitinating enzymes that are recruited to sites of DNA damage, ensure proper local polyubiquitin chain composition for downstream DNA repair protein assembly. Their study offers a key insight into the mechanism of crosstalk between linkage-specific ubiquitylation at DNA damage sites, while simultaneously raising important questions for future research.
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Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.334383.119.
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