Journal
EMBO REPORTS
Volume 15, Issue 5, Pages 601-608Publisher
WILEY
DOI: 10.1002/embr.201338369
Keywords
SUMO-targeted E3 ubiquitin ligase (STUbL); small ubiquitin-like modifier; RNF4; ubiquitin; telomere
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Funding
- Leukemia & Lymphoma Society
- NIH [GM068608, GM081840, GM088409, AR059968, AG038677]
- Pew Scholars Award
- Novartis Advanced Discovery Institute
- IDAT program - DOE Office of Biological and Environmental Research plus NIH Grants [GM105404, CA092584]
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The post-translational modification of DNA repair and checkpoint proteins by ubiquitin and small ubiquitin-like modifier (SUMO) critically orchestrates the DNA damage response (DDR). The ubiquitin ligase RNF4 integrates signaling by SUMO and ubiquitin, through its selective recognition and ubiquitination of SUMO-modified proteins. Here, we define a key new determinant for target discrimination by RNF4, in addition to interaction with SUMO. We identify a nucleosome-targeting motif within the RNF4 RING domain that can bind DNA and thereby enables RNF4 to selectively ubiquitinate nucleosomal histones. Furthermore, RNF4 nucleosome-targeting is crucially required for the repair of TRF2-depleted dysfunctional telomeres by 53BP1-mediated non-homologous end joining.
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