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SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Author

Listed:
  • 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)

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.

Suggested Citation

  • 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 Ve, 2015. "SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8499
    DOI: 10.1038/ncomms8499
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    Cited by:

    1. Diana A. Llerena Schiffmacher & Shun-Hsiao Lee & Katarzyna W. Kliza & Arjan F. Theil & Masaki Akita & Angela Helfricht & Karel Bezstarosti & Camila Gonzalo-Hansen & Haico Attikum & Matty Verlaan-de Vr, 2024. "The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Andrej Paluda & Adam J. Middleton & Claudia Rossig & Peter D. Mace & Catherine L. Day, 2022. "Ubiquitin and a charged loop regulate the ubiquitin E3 ligase activity of Ark2C," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

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