Phosphorylation of telomeric repeat binding factor 1 (TRF1) by Akt causes telomere shortening.

@article{Chen2009PhosphorylationOT,
  title={Phosphorylation of telomeric repeat binding factor 1 (TRF1) by Akt causes telomere shortening.},
  author={Yen-Chung Chen and S Teng and Kou-Juey Wu},
  journal={Cancer investigation},
  year={2009},
  volume={27 1},
  pages={24-8}
}
Telomeric repeat binding factor 1 (TRF1) belongs to the shelterin complex, which modulates the telomere structures. Akt/protein kinase B activation caused genomic instability and contributes to tumorigenesis, although the molecular mechanism remained little known. Here, we show the direct interaction between Akt and TRF1. In vitro kinase assays showed the phosphorylation of a putative Akt phosphorylation site (Threonine 273) in wild type TRF1, but not the mutant TRF1 (T273A), by Akt… CONTINUE READING
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