Ku80 facilitates chromatin binding of the telomere binding protein, TRF2

The Ku70/80 heterodimer is central to non-homologous end joining repair of DNA double-strand breaks and the Ku80 gene appears to be essential for human but not rodent cell survival. The Ku70/80 heterodimer is located at telomeres but its precise function in telomere maintenance is not known.  In ord...

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Bibliographic Details
Published in:Cell cycle (Georgetown, Tex.) Tex.), 2010-09, Vol.9 (18), p.3822-3830
Main Authors: Fink, Lauren S., Lerner, Chad A., Torres, Paulina F., Sell, Christian
Format: Article
Language:English
Subjects:
Antigens, Nuclear - genetics
Antigens, Nuclear - metabolism
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Chromatin - metabolism
Cycle
Dimerization
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Fibroblasts - metabolism
Humans
Ku Autoantigen
Landes
Organogenesis
Proteasome Endopeptidase Complex - metabolism
Protein Binding
Proteins
RNA Interference
Telomere - metabolism
Telomeric Repeat Binding Protein 2 - metabolism
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Summary:The Ku70/80 heterodimer is central to non-homologous end joining repair of DNA double-strand breaks and the Ku80 gene appears to be essential for human but not rodent cell survival. The Ku70/80 heterodimer is located at telomeres but its precise function in telomere maintenance is not known.  In order to examine the role of Ku80 fibroblast strain.  Following targeted Ku80 knockdown, telomere defects are observed and the steady state levels of the TRF2 protein are reduced. Inhibitor studies indicate that this loss of TRF2 is mediated by the proteasome, and degradation of TRF2 following Ku depletion appears to involve a decrease in chromatin binding of TRF2, suggesting that the Ku heterodimer enhances TRF2 chromatin association and that non-chromatin bound TRF2 is targeted to the proteasome.
ISSN:1538-4101
1551-4005
DOI:10.4161/cc.9.18.13129