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

Authors :
Velma V
Carrero ZI
Cosman AM
Hebert MD
Source :
FEBS letters [FEBS Lett] 2010 Dec 01; Vol. 584 (23), pp. 4735-9. Date of Electronic Publication: 2010 Nov 09.
Publication Year :
2010

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.<br /> (Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1873-3468
Volume :
584
Issue :
23
Database :
MEDLINE
Journal :
FEBS letters
Publication Type :
Academic Journal
Accession number :
21070772
Full Text :
https://doi.org/10.1016/j.febslet.2010.11.004