This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Huda, N.
Right arrow Articles by Gilley, D.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huda, N.
Right arrow Articles by Gilley, D.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, July 2009, p. 3597-3604, Vol. 29, No. 13
0270-7306/09/$08.00+0     doi:10.1128/MCB.00944-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

DNA Damage-Induced Phosphorylation of TRF2 Is Required for the Fast Pathway of DNA Double-Strand Break Repair{triangledown}

Nazmul Huda,1,# Hiromi Tanaka,1,# Marc S. Mendonca,1,2 and David Gilley1*

Department of Medical and Molecular Genetics,1 Department of Radiation Oncology, Indiana University School of Medicine, Indianapolis, Indiana 462022

Received 13 June 2008/ Returned for modification 18 August 2008/ Accepted 14 April 2009

Protein kinases of the phosphatidylinositol 3-kinase-like kinase family, originally known to act in maintaining genomic integrity via DNA repair pathways, have been shown to also function in telomere maintenance. Here we focus on the functional role of DNA damage-induced phosphorylation of the essential mammalian telomeric DNA binding protein TRF2, which coordinates the assembly of the proteinaceous cap to disguise the chromosome end from being recognized as a double-stand break (DSB). Previous results suggested a link between the transient induction of human TRF2 phosphorylation at threonine 188 (T188) by the ataxia telangiectasia mutated protein kinase (ATM) and the DNA damage response. Here, we report evidence that X-ray-induced phosphorylation of TRF2 at T188 plays a role in the fast pathway of DNA DSB repair. These results connect the highly transient induction of human TRF2 phosphorylation to the DNA damage response machinery. Thus, we find that a protein known to function in telomere maintenance, TRF2, also plays a functional role in DNA DSB repair.


* Corresponding author. Mailing address: IB-130, 975 West Walnut Street, Indianapolis, IN 46202. Phone: (317) 278-9158. Fax: (317) 274-1069. E-mail: DPGilley{at}iupui.edu

{triangledown} Published ahead of print on 27 April 2009.

# These authors contributed equally to this work.


Molecular and Cellular Biology, July 2009, p. 3597-3604, Vol. 29, No. 13
0270-7306/09/$08.00+0     doi:10.1128/MCB.00944-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.