XRCC1 protein; Form and function |
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| Affiliation: | 1. Genome Damage and Stability Centre, School of Life Sciences, Falmer, Brighton, BN1 9RQ, United Kingdom;2. Department of Genome Dynamics, Institute of Molecular Genetics of the Czech Academy of Sciences, 142 20, Prague, 4, Czech Republic;1. Department of Pharmacological Sciences, State University of New York at Stony Brook, Stony Brook, New York, 11794, USA;2. Biochemistry and Structural Biology graduate program, Stony Brook University, New York 11794, USA;3. Stony Brook Cancer Center, Renaissance School of Medicine at Stony Brook University, Stony Brook, New York, 11794, USA;1. Department of Physiology and Cell Biology, University of South Alabama College of Medicine, Mobile, AL, USA;2. Mitchell Cancer Institute, University of South Alabama, Mobile, AL, USA;1. Genome Integrity and Structural Biology Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA;2. Fluorescence Microscopy and Imaging Center, Signal Transduction Laboratory, NIEHS, National Institutes of Health, Research Triangle Park, NC 27709, USA;3. Department of Oncologic Sciences, University of South Alabama Mitchell Cancer Institute, Mobile, AL 36604, USA;1. Department of Oral and Maxillofacial Medicine, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;2. Students Research Committee, Kermanshah University of Medical Sciences, Kermanshah 6715847141, Iran;3. Department of Endodontics, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;4. Advanced Dental Sciences Research Center, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;5. Dermatology Unit, Department of Translational Medicine, University of Eastern Piedmont, Novara 28100, Italy;6. School of Dentistry and Oral Health, Menzies Health Institute Queensland, Griffith University, Gold Coast 4214, Australia;7. Department of Orthodontics, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;8. Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah 6714415185, Iran;9. Department of Prosthodontics, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;10. Department of Oral and Maxillofacial Surgery, School of Dentistry, Kermanshah University of Medical Sciences, Kermanshah 6713954658, Iran;1. Laboratory for Advanced Nuclear Energy, Institute of Innovative Research, Tokyo Institute of Technology, 2-12-1 Oookayama, Meguro-ku, Tokyo, 152-8550, Japan;2. National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo, 104-0045, Japan |
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| Abstract: | The human gene that encodes XRCC1 was cloned nearly thirty years ago but experimental analysis of this fascinating protein is still unveiling new insights into the DNA damage response. XRCC1 is a molecular scaffold protein that interacts with multiple enzymatic components of DNA single-strand break repair (SSBR) including DNA kinase, DNA phosphatase, DNA polymerase, DNA deadenylase, and DNA ligase activities that collectively are capable of accelerating the repair of a broad range of DNA single-strand breaks (SSBs). Arguably the most exciting aspect of XRCC1 function that has emerged in the last few years is its intimate relationship with PARP1 activity and critical role in preventing hereditary neurodegenerative disease. Here, I provide an update on our current understanding of XRCC1, and on the impact of hereditary mutations in this protein and its protein partners on human disease. |
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| Keywords: | DNA single-strand break (SSB) DNA double-strand break (DSB) Single-strand break repair (SSBR) Double-strand break repair (DSBR) Non-homologous end-joining (NHEJ) |
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