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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...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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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. |
format | Online Article Text |
id | pubmed-4455304 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
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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