SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Loes van Cuijk, Gijsbert J. van Belle, Yasemin Turkyilmaz, Sara L. Poulsen, Roel C. Janssens, Arjan F. Theil, Mariangela Sabatella, Hannes Lans, Niels Mailand, Adriaan B. Houtsmuller, Wim Vermeulen and Jurgen A. Marteijn ()
Additional contact information
Loes van Cuijk: Cancer Genomics Netherlands Erasmus MC
Gijsbert J. van Belle: Josephine Nefkens Institute, Erasmus MC
Yasemin Turkyilmaz: Cancer Genomics Netherlands Erasmus MC
Sara L. Poulsen: Ubiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen
Roel C. Janssens: Cancer Genomics Netherlands Erasmus MC
Arjan F. Theil: Cancer Genomics Netherlands Erasmus MC
Mariangela Sabatella: Cancer Genomics Netherlands Erasmus MC
Hannes Lans: Cancer Genomics Netherlands Erasmus MC
Niels Mailand: Ubiquitin Signaling Group, Protein Signaling Program, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen
Adriaan B. Houtsmuller: Josephine Nefkens Institute, Erasmus MC
Wim Vermeulen: Cancer Genomics Netherlands Erasmus MC
Jurgen A. Marteijn: Cancer Genomics Netherlands Erasmus MC

Nature Communications, 2015, vol. 6, issue 1, 1-10

Abstract: Abstract XPC recognizes UV-induced DNA lesions and initiates their removal by nucleotide excision repair (NER). Damage recognition in NER is tightly controlled by ubiquitin and SUMO modifications. Recent studies have shown that the SUMO-targeted ubiquitin ligase RNF111 promotes K63-linked ubiquitylation of SUMOylated XPC after DNA damage. However, the exact regulatory function of these modifications in vivo remains elusive. Here we show that RNF111 is required for efficient repair of ultraviolet-induced DNA lesions. RNF111-mediated ubiquitylation promotes the release of XPC from damaged DNA after NER initiation, and is needed for stable incorporation of the NER endonucleases XPG and ERCC1/XPF. Our data suggest that RNF111, together with the CRL4DDB2 ubiquitin ligase complex, is responsible for sequential XPC ubiquitylation, which regulates the recruitment and release of XPC and is crucial for efficient progression of the NER reaction, thereby providing an extra layer of quality control of NER.

Date: 2015
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DOI: 10.1038/ncomms8499

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