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RESEARCH HIGHLIGHTS
endogenous and exogenous TRF2 in primary human fibroblasts, which indicates that these proteins interact in vivo.Pulldown experiments using fusion proteins that comprised different fragments of ATM showed that TRF2 bound to a specific domain of ATM, close to serine 1981 the main site of autophosphorylation. Finally, immunofluorescence of IR-treated primary fibroblasts that overexpressed TRF2 detected the protein at telom-eric foci, but not at chromosomal sites of DNA damage.
Based on these results, the authors propose a model in which TRF2 binds to ATM and inhibits its activation by preventing phosphorylation at S1981. Importantly, the subnuclear location of TRF2 indicates that this inhibition is restricted to telomeres, which would allow ATM to mediate vital DNA repair elsewhere in the nucleus.
Shannon Amoils References and links
ORIGINAL RESEARCH PAPER Karlseder, J. et al. The telomeric protein TRF2 binds the ATM kinase and can inhibit the ATM-dependent DNA damage response. PLoS Biology 2, 11501156 (2004)
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