Journal
CANCER INVESTIGATION
Volume 27, Issue 1, Pages 24-28Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07357900802027081
Keywords
TRF1; Akt; Phosphorylation; Telomere regulation
Categories
Funding
- National Research Program for Genomic Medicine [NRPGM-DOH-96-TD-G-111-002]
- National Science Council [NSC95-2320-B-010-065]
- National Health Research Institutes [NHRI-EX97-9611BI, NHRI-EX95-9329SI]
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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. Overexpression of Akt decreased telomere length in a HTC cell line. These results indicate that Akt plays an important role in telomere length regulation, contributing to genomic instability and tumorigenesis.
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