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

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.

Pubmed ID: 15231715

Authors

  • Ye JZ
  • Hockemeyer D
  • Krutchinsky AN
  • Loayza D
  • Hooper SM
  • Chait BT
  • de Lange T

Journal

Genes & development

Publication Data

July 15, 2004

Associated Grants

  • Agency: NCI NIH HHS, Id: K08 CA93604
  • Agency: NCRR NIH HHS, Id: RR00862
  • Agency: NCI NIH HHS, Id: T32 CA09673-26A1

Mesh Terms

  • Carrier Proteins
  • Cloning, Molecular
  • Fluorescent Antibody Technique
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mass Spectrometry
  • RNA Interference
  • Telomere
  • Telomere-Binding Proteins
  • Telomeric Repeat Binding Protein 1
  • Two-Hybrid System Techniques