SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Loes Cuijk; Bert-Jaap Belle; Yasemin Türkyilmaz; SL Poulsen; Roel Janssens; Arjan Theil; Mariangela Sabatella; Hannes Lans; N Mailand; Adriaan Houtsmuller; Wim Vermeulen; Jurgen Marteijn

doi:10.1038/ncomms8499

SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Loes Cuijk, Bert-Jaap Belle, Yasemin Türkyilmaz, SL Poulsen, Roel Janssens, Arjan Theil, Mariangela Sabatella, Hannes Lans, N Mailand, Adriaan Houtsmuller, Wim Vermeulen, Jurgen Marteijn

Research output: Contribution to journal › Article › Academic › peer-review

90 Citations (Scopus)

12 Downloads (Pure)

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 CRL4(DDB2) 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.

Original language	English
Journal	Nature Communications
Volume	6
DOIs	https://doi.org/10.1038/ncomms8499
Publication status	Published - 2015

Research programs

EMC MGC-01-12-03
EMC MM-03-24-01

Access to Document

10.1038/ncomms8499

REPUB_86484-OA.pdfFinal published version, 1.32 MB

http://hdl.handle.net/1765/86484

Cite this

@article{a9b1247cb14c407482718ec7ced5ba8c,

title = "SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair",

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 CRL4(DDB2) 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.",

author = "Loes Cuijk and Bert-Jaap Belle and Yasemin T{\"u}rkyilmaz and SL Poulsen and Roel Janssens and Arjan Theil and Mariangela Sabatella and Hannes Lans and N Mailand and Adriaan Houtsmuller and Wim Vermeulen and Jurgen Marteijn",

year = "2015",

doi = "10.1038/ncomms8499",

language = "English",

volume = "6",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "Nature Research",

}

TY - JOUR

T1 - SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

AU - Cuijk, Loes

AU - Belle, Bert-Jaap

AU - Türkyilmaz, Yasemin

AU - Poulsen, SL

AU - Janssens, Roel

AU - Theil, Arjan

AU - Sabatella, Mariangela

AU - Lans, Hannes

AU - Mailand, N

AU - Houtsmuller, Adriaan

AU - Vermeulen, Wim

AU - Marteijn, Jurgen

PY - 2015

Y1 - 2015

N2 - 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 CRL4(DDB2) 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.

AB - 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 CRL4(DDB2) 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.

U2 - 10.1038/ncomms8499

DO - 10.1038/ncomms8499

M3 - Article

C2 - 26151477

SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

ER -

SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Abstract

Research programs

Access to Document

Fingerprint

Cite this