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Nucleic Acids Research Advance Access published online on August 9, 2007
Nucleic Acids Research, doi:10.1093/nar/gkm550
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© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Ubiquitylation-independent degradation of Xeroderma pigmentosum group C protein is required for efficient nucleotide excision repair

Qi-En Wang1,*, Mette Prætorius-Ibba1, Qianzheng Zhu1, Mohamed A. El-Mahdy1, Gulzar Wani1, Qun Zhao1, Song Qin1, Srinivas Patnaik1 and Altaf A. Wani1,2,3,*

1Department of Radiology, 2Department of Molecular and Cellular Biochemistry and 3Comprehensive Cancer Center, The Ohio State University, 460 W. 12th Ave, Columbus, OH 43210, USA

*To whom correspondence should be addressed. Tel: +1 614 292 9015; Fax: +1 614 293 0802; Email: wang.771{at}osu.edu; wani.2{at}osu.edu

Received March 13, 2007. Revised June 27, 2007. Accepted July 5, 2007.

The Xeroderma Pigmentosum group C (XPC) protein is indispensable to global genomic repair (GGR), a subpathway of nucleotide excision repair (NER), and plays an important role in the initial damage recognition. XPC can be modified by both ubiquitin and SUMO in response to UV irradiation of cells. Here, we show that XPC undergoes degradation upon UV irradiation, and this is independent of protein ubiquitylation. The subunits of DDB-Cul4A E3 ligase differentially regulate UV-induced XPC degradation, e.g DDB2 is required and promotes, whereas DDB1 and Cul4A protect the protein degradation. Mutation of XPC K655 to alanine abolishes both UV-induced XPC modification and degradation. XPC degradation is necessary for recruiting XPG and efficient NER. The overall results provide crucial insights regarding the fate and role of XPC protein in the initiation of excision repair.


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