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; Jurgen A. Marteijn

doi:10.1038/ncomms8499

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, Jurgen A. Marteijn

Onderzoeksoutput: Bijdrage aan tijdschrift › Artikel › peer review

90 Citaten (Scopus)

Samenvatting

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.

Originele taal-2	Engels
Artikelnummer	7499
Tijdschrift	Nature Communications
Volume	6
DOI's	https://doi.org/10.1038/ncomms8499
Status	Gepubliceerd - 7 jul. 2015
Extern gepubliceerd	Ja

Toegang tot document

10.1038/ncomms8499

Citeer dit

@article{5d0c101f59ce4bc6bddfa49c20131a2b,

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 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.",

author = "{Van Cuijk}, Loes and {Van Belle}, {Gijsbert J.} and Yasemin Turkyilmaz and Poulsen, {Sara L.} and Janssens, {Roel C.} and Theil, {Arjan F.} and Mariangela Sabatella and Hannes Lans and Niels Mailand and Houtsmuller, {Adriaan B.} and Wim Vermeulen and Marteijn, {Jurgen A.}",

note = "Funding Information: We thank Dr V. Episkopou for providing RNF111−/− primary mouse fibroblasts. This work was supported by the Dutch Organization for Scientific Research ZonMW TOP Grants (912.08.031and 912.12.132), Dutch Organization for Scientific Research ALW VIDI grant (846.13.004), Horizon Zenith (935.11.042), Dutch Science Organization (NWO), Chemical Sciences (CW), ECHO.12.B1.043, European Research Council Advanced Grant (340988-ERC-ID), FP7 Marie Curie International Training Network aDDRess and Erasmus MC fellowship.",

year = "2015",

month = jul,

day = "7",

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 - Van Cuijk, Loes

AU - Van Belle, Gijsbert J.

AU - Turkyilmaz, Yasemin

AU - Poulsen, Sara L.

AU - Janssens, Roel C.

AU - Theil, Arjan F.

AU - Sabatella, Mariangela

AU - Lans, Hannes

AU - Mailand, Niels

AU - Houtsmuller, Adriaan B.

AU - Vermeulen, Wim

AU - Marteijn, Jurgen A.

N1 - Funding Information: We thank Dr V. Episkopou for providing RNF111−/− primary mouse fibroblasts. This work was supported by the Dutch Organization for Scientific Research ZonMW TOP Grants (912.08.031and 912.12.132), Dutch Organization for Scientific Research ALW VIDI grant (846.13.004), Horizon Zenith (935.11.042), Dutch Science Organization (NWO), Chemical Sciences (CW), ECHO.12.B1.043, European Research Council Advanced Grant (340988-ERC-ID), FP7 Marie Curie International Training Network aDDRess and Erasmus MC fellowship.

PY - 2015/7/7

Y1 - 2015/7/7

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 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.

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 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.

UR - http://www.scopus.com/inward/record.url?scp=84936745419&partnerID=8YFLogxK

U2 - 10.1038/ncomms8499

DO - 10.1038/ncomms8499

M3 - Article

C2 - 26151477

AN - SCOPUS:84936745419

SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

M1 - 7499

ER -

SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair

Samenvatting

Toegang tot document

Vingerafdruk

Citeer dit