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SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair

The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in v...

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Autores principales: Akita, Masaki, Tak, Yon-Soo, Shimura, Tsutomu, Matsumoto, Syota, Okuda-Shimizu, Yuki, Shimizu, Yuichiro, Nishi, Ryotaro, Saitoh, Hisato, Iwai, Shigenori, Mori, Toshio, Ikura, Tsuyoshi, Sakai, Wataru, Hanaoka, Fumio, Sugasawa, Kaoru
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4455304/
https://www.ncbi.nlm.nih.gov/pubmed/26042670
http://dx.doi.org/10.1038/srep10984
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author Akita, Masaki
Tak, Yon-Soo
Shimura, Tsutomu
Matsumoto, Syota
Okuda-Shimizu, Yuki
Shimizu, Yuichiro
Nishi, Ryotaro
Saitoh, Hisato
Iwai, Shigenori
Mori, Toshio
Ikura, Tsuyoshi
Sakai, Wataru
Hanaoka, Fumio
Sugasawa, Kaoru
author_facet Akita, Masaki
Tak, Yon-Soo
Shimura, Tsutomu
Matsumoto, Syota
Okuda-Shimizu, Yuki
Shimizu, Yuichiro
Nishi, Ryotaro
Saitoh, Hisato
Iwai, Shigenori
Mori, Toshio
Ikura, Tsuyoshi
Sakai, Wataru
Hanaoka, Fumio
Sugasawa, Kaoru
author_sort Akita, Masaki
collection PubMed
description The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER.
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spelling pubmed-44553042015-06-10 SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair Akita, Masaki Tak, Yon-Soo Shimura, Tsutomu Matsumoto, Syota Okuda-Shimizu, Yuki Shimizu, Yuichiro Nishi, Ryotaro Saitoh, Hisato Iwai, Shigenori Mori, Toshio Ikura, Tsuyoshi Sakai, Wataru Hanaoka, Fumio Sugasawa, Kaoru Sci Rep Article The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER. Nature Publishing Group 2015-06-04 /pmc/articles/PMC4455304/ /pubmed/26042670 http://dx.doi.org/10.1038/srep10984 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Akita, Masaki
Tak, Yon-Soo
Shimura, Tsutomu
Matsumoto, Syota
Okuda-Shimizu, Yuki
Shimizu, Yuichiro
Nishi, Ryotaro
Saitoh, Hisato
Iwai, Shigenori
Mori, Toshio
Ikura, Tsuyoshi
Sakai, Wataru
Hanaoka, Fumio
Sugasawa, Kaoru
SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title_full SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title_fullStr SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title_full_unstemmed SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title_short SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
title_sort sumoylation of xeroderma pigmentosum group c protein regulates dna damage recognition during nucleotide excision repair
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4455304/
https://www.ncbi.nlm.nih.gov/pubmed/26042670
http://dx.doi.org/10.1038/srep10984
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