4.7 Article

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

Journal

GENES & DEVELOPMENT
Volume 18, Issue 14, Pages 1649-1654

Publisher

COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1215404

Keywords

telomere; telomerase; TRF1; TIN2; POT1; PIP1

Funding

  1. NCI NIH HHS [T32 CA009673, K08 CA093604, T32 CA09673-26A1, K08 CA93604] Funding Source: Medline
  2. NCRR NIH HHS [P41 RR000862, RR00862] Funding Source: Medline

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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.

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