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^*

^*Corresponding author for this work

61 Citations (Scopus)

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<sup>DDB2</sup> 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
Article number	7499
Journal	Nature Communications
Volume	6
Number of pages	10
ISSN	2041-1723
DOIs	https://doi.org/10.1038/ncomms8499
Publication status	Published - 7 Jul 2015

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@article{35054206afae45e6bf4bcc12926d306b,

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.}",

year = "2015",

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doi = "10.1038/ncomms8499",

language = "English",

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journal = "Nature Communications",

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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.

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.

U2 - 10.1038/ncomms8499

DO - 10.1038/ncomms8499

M3 - Journal 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

Abstract

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