POT1-interacting protein PIP1: a telomere length regulator that recruits POT1 to the TIN2/TRF1 complex

被引:348
作者
Ye, JZS
Hockemeyer, D
Krutchinsky, AN
Loayza, D
Hooper, SM
Chait, BT
de Lange, T
机构
[1] Rockefeller Univ, Lab Mass Spect & Gaseous Ion Chem, New York, NY 10021 USA
[2] Mem Sloan Kettering Canc Ctr, Dept Med, New York, NY 10021 USA
[3] Rockefeller Univ, Cell Biol & Genet Lab, New York, NY 10021 USA
关键词
telomere; telomerase; TRF1; TIN2; POT1; PIP1;
D O I
10.1101/gad.1215404
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Human telomere length is controlled by a negative feedback loop based on the binding of TRF1 to double-stranded telomeric DNA. The TRF1 complex recruits POT1, a single-stranded telomeric DNA-binding protein necessary for cis-inhibition of telomerase. By mass spectrometry, we have identified a new telomeric protein, which we have named POT1-interacting protein 1 (PIP1). PIP1 bound both POT1 and the TRF1-interacting factor TIN2 and could tether POT1 to the TRF1 complex. Reduction of PIP1 or POT1 levels with shRNAs led to telomere elongation, indicating that PIP1 contributes to telomere length control through recruitment of POT1.
引用
收藏
页码:1649 / 1654
页数:6
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