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• Hanssen-Bauer, A
• Solvang-Garten, K
• Akbari, M
• Otterlei, M
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• Hanssen-Bauer, A
• Solvang-Garten, K
• Akbari, M
• Otterlei, M
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• Hanssen-Bauer, A
• Solvang-Garten, K
• Akbari, M
• Otterlei, M

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Int. J. Mol. Sci. 2012, 13(12), 17210-17229; doi:10.3390/ijms131217210

Review

X-Ray Repair Cross Complementing Protein 1 in Base Excision Repair

Audun Hanssen-Bauer ¹ , Karin Solvang-Garten ¹ , Mansour Akbari ²  and Marit Otterlei ^1,*

¹ Department of Cancer Research and Molecular Medicine, Faculty of Medicine, Norwegian University of Science and Technology, N-7489 Trondheim, Norway ² Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 N, Denmark

* Author to whom correspondence should be addressed.

Received: 9 November 2012; in revised form: 6 December 2012 / Accepted: 7 December 2012 / Published: 17 December 2012

(This article belongs to the Special Issue DNA Damage and Repair in Degenerative Diseases)

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Abstract: X-ray Repair Cross Complementing protein 1 (XRCC1) acts as a scaffolding protein in the converging base excision repair (BER) and single strand break repair (SSBR) pathways. XRCC1 also interacts with itself and rapidly accumulates at sites of DNA damage. XRCC1 can thus mediate the assembly of large multiprotein DNA repair complexes as well as facilitate the recruitment of DNA repair proteins to sites of DNA damage. Moreover, XRCC1 is present in constitutive DNA repair complexes, some of which associate with the replication machinery. Because of the critical role of XRCC1 in DNA repair, its common variants Arg194Trp, Arg280His and Arg399Gln have been extensively studied. However, the prevalence of these variants varies strongly in different populations, and their functional influence on DNA repair and disease remains elusive. Here we present the current knowledge about the role of XRCC1 and its variants in BER and human disease/cancer.

Keywords: BER; XRCC1; disease; DNA damage; polymorphisms; recruitment; repair complex; scaffold

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