Coilin interacts with Ku proteins and inhibits in vitro non-homologous DNA end joining

FEBS Lett. 2010 Dec 1;584(23):4735-9. doi: 10.1016/j.febslet.2010.11.004. Epub 2010 Nov 9.

Abstract

Coilin is a nuclear protein that plays a role in Cajal body formation. The function of nucleoplasmic coilin is unknown. Here we report that coilin interacts with Ku70 and Ku80, which are major players in the DNA repair process. Ku proteins compete with SMN and SmB' proteins for coilin interaction sites. The binding domain on coilin for Ku proteins cannot be localized to one discrete region, and only full-length coilin is capable of inhibiting in vitro non-homologous DNA end joining (NHEJ). Since Ku proteins do not accumulate in CBs, these findings suggest that nucleoplasmic coilin participates in the regulation of DNA repair.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Binding, Competitive
  • DNA Helicases / metabolism*
  • DNA Repair / drug effects*
  • HeLa Cells
  • Humans
  • Ku Autoantigen
  • Nuclear Proteins / metabolism*
  • Nuclear Proteins / pharmacology*
  • Recombination, Genetic / drug effects*
  • Survival of Motor Neuron 1 Protein / metabolism
  • snRNP Core Proteins / metabolism

Substances

  • Nuclear Proteins
  • SNRPB protein, human
  • Survival of Motor Neuron 1 Protein
  • snRNP Core Proteins
  • p80-coilin
  • DNA Helicases
  • XRCC5 protein, human
  • Ku Autoantigen