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EMBO Rep. 2014 May;15(5):601-8. doi: 10.1002/embr.201338369. Epub 2014 Apr 8.

RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response.

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1
Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA, USA.

Abstract

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.

PMID:
24714598
PMCID:
PMC4210088
DOI:
10.1002/embr.201338369
[Indexed for MEDLINE]
Free PMC Article

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