Collaboration and competition between DNA double-strand break repair pathways Journal Article

   


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:

http://www.scopus.com/inward/record.url?eid=2-s2.0-77955841149&partnerID=40&md5=0ba75ada983afb0fc7ffe54cc4432d98
Notes: --- - "Cited By (since 1996): 3" - "Export Date: 20 April 2011" - "CODEN: FEBLA" - "Source: Scopus"
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MSK Authors
  1. Maria Jasin
    250 Jasin
  2. Elizabeth M Kass
    13 Kass
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