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• W2162227162 abstract "TRF2 is a component of shelterin, the telomere-specific protein complex that prevents DNA damage signaling and inappropriate repair at the natural ends of mammalian chromosomes. We describe a temperature-sensitive (ts) mutation in the Myb/SANT DNA-binding domain of TRF2 that allows controlled and reversible telomere deprotection. At 32°C, TRF2ts was functional and rescued the lethality of TRF2 deletion from conditional TRF2 F/− mouse embryonic fibroblasts (MEFs). When shifted to the nonpermissive temperature (37°C), TRF2ts cells showed extensive telomere damage resulting in activation of the ATM kinase and nonhomologous end-joining (NHEJ) of chromosome ends. The inactivation of TRF2ts at 37°C was rapid and reversible, permitting induction of short periods (3–6 h) of telomere dysfunction in the G0, G1, and S/G2 phases of the cell cycle. The results indicate that both the induction of telomere dysfunction and the re-establishment of the protected state can take place throughout interphase. In contrast, the processing of dysfunctional telomeres by NHEJ occurred primarily in G1, being repressed in S/G2 in a cyclin-dependent kinase (CDK)-dependent manner." @default.
• W2162227162 created "2016-06-24" @default.
• W2162227162 creator A5060775773 @default.
• W2162227162 creator A5065113600 @default.
• W2162227162 date "2008-05-01" @default.
• W2162227162 modified "2023-10-17" @default.
• W2162227162 title "Cell cycle control of telomere protection and NHEJ revealed by a ts mutation in the DNA-binding domain of TRF2" @default.
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• W2162227162 doi "https://doi.org/10.1101/gad.1634008" @default.
• W2162227162 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2335317" @default.
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