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

  1. Jeffrey Zheng-Sheng Ye1,3,4,5,
  2. Dirk Hockemeyer1,
  3. Andrew N. Krutchinsky2,
  4. Diego Loayza1,
  5. Sarah M. Hooper1,
  6. Brian T. Chait2, and
  7. Titia de Lange1,6
  1. 1Laboratory for Cell Biology and Genetics and 2Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10021, USA; 3Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA

Abstract

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.

Keywords

Footnotes

  • Supplemental material is available at http://www.genesdev.org.

  • Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1215404.

  • Corresponding authors.

  • ↵4 Present address: Division of Hematology, Departments of Medicine and Pharmacology, New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA.

  • ↵5 E-MAIL jeffrey.ye{at}med.nyu.edu; FAX (212) 263-8444.

  • ↵6 E-MAIL delange{at}mail.rockefeller.edu; FAX (212) 327-7147.

    • Accepted May 14, 2004.
    • Received April 26, 2004.
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  1. Published in Advance July 1, 2004, doi: 10.1101/gad.1215404 Genes & Dev. 2004. 18: 1649-1654 Copyright © 2004, by Cold Spring Harbor Laboratory Press

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