Authors: | Kass, E. M.; Jasin, M. |
Article Title: | Collaboration and competition between DNA double-strand break repair pathways |
Abstract: | DNA double-strand breaks resulting from normal cellular processes including replication and exogenous sources such as ionizing radiation pose a serious risk to genome stability, and cells have evolved different mechanisms for their efficient repair. The two major pathways involved in the repair of double-strand breaks in eukaryotic cells are non-homologous end joining and homologous recombination. Numerous factors affect the decision to repair a double-strand break via these pathways, and accumulating evidence suggests these major repair pathways both cooperate and compete with each other at double-strand break sites to facilitate efficient repair and promote genomic integrity. © 2010 Federation of European Biochemical Societies. |
Keywords: | gene mutation; mutation; review; nonhuman; dna replication; animals; mre11 protein; rad50 protein; dna damage; homologous recombination; cell cycle; dna repair; protein protein interaction; brca1 protein; brca2 protein; excision repair cross complementing protein 1; nibrin; dna; conserved sequence; brain; saccharomyces cerevisiae; eukaryota; recombination, genetic; genomic instability; genes, brca1; genes, brca2; dna breaks, double-stranded; rad54 protein; double stranded dna break; base sequence; replication factor a; ku antigen; xrcc4 protein; homeostasis; cyclin dependent kinase; cell cycle regulation; histone h2ax; rad51 protein; fanconi anemia; non-homologous end joining; fanconi anemia group d2 protein; rad52 protein; double-strand break; single-strand annealing; dna dependent protein kinase; fanconi anemia group c protein; protein rad1 |
Journal Title: | FEBS Letters |
Volume: | 584 |
Issue: | 17 |
ISSN: | 0014-5793 |
Publisher: | Wiley Blackwell |
Date Published: | 2010-09-10 |
Start Page: | 3703 |
End Page: | 3708 |
Language: | English |
DOI: | 10.1016/j.febslet.2010.07.057 |
PUBMED: | 20691183 |
PROVIDER: | scopus |
PMCID: | PMC3954739 |
DOI/URL: | |
Notes: | --- - "Cited By (since 1996): 3" - "Export Date: 20 April 2011" - "CODEN: FEBLA" - "Source: Scopus" |