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DNA Repair (Amst). 2014 May;17:30-8. doi: 10.1016/j.dnarep.2014.02.019. Epub 2014 Mar 26.

One ring to bring them all--the role of Ku in mammalian non-homologous end joining.

Author information

1
Genome Damage and Stability Centre, Science Park Road, Falmer, Brighton BN1 9RQ, UK. Electronic address: g.j.grundy@sussex.ac.uk.
2
School of Biochemistry, Medical Sciences, University Walk, Bristol BS8 1TD, UK.
3
Genome Damage and Stability Centre, Science Park Road, Falmer, Brighton BN1 9RQ, UK. Electronic address: k.w.caldecott@sussex.ac.uk.
4
Genome Damage and Stability Centre, Science Park Road, Falmer, Brighton BN1 9RQ, UK. Electronic address: s.l.rulten@sussex.ac.uk.

Abstract

The repair of DNA double strand breaks is essential for cell survival and several conserved pathways have evolved to ensure their rapid and efficient repair. The non-homologous end joining pathway is initiated when Ku binds to the DNA break site. Ku is an abundant nuclear heterodimer of Ku70 and Ku80 with a toroidal structure that allows the protein to slide over the broken DNA end and bind with high affinity. Once locked into placed, Ku acts as a tool-belt to recruit multiple interacting proteins, forming one or more non-homologous end joining complexes that act in a regulated manner to ensure efficient repair of DNA ends. Here we review the structure and functions of Ku and the proteins with which it interacts during non-homologous end joining.

KEYWORDS:

APLF; Double-strand break; Ku; Non-homologous end joining; WRN

PMID:
24680220
DOI:
10.1016/j.dnarep.2014.02.019
[Indexed for MEDLINE]

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