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 te...

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Bibliographic Details
Published in:Genes & development 2004-07, Vol.18 (14), p.1649-1654
Main Authors: Ye, Jeffrey Zheng-Sheng, Hockemeyer, Dirk, Krutchinsky, Andrew N, Loayza, Diego, Hooper, Sarah M, Chait, Brian T, de Lange, Titia
Format: Article
Language:English
Subjects:
Carrier Proteins - metabolism
Cloning, Molecular
Fluorescent Antibody Technique
HeLa Cells
Humans
Intracellular Signaling Peptides and Proteins
Mass Spectrometry
Research Communications
RNA Interference
Shelterin Complex
Telomere - metabolism
Telomere - physiology
Telomere-Binding Proteins - metabolism
Telomeric Repeat Binding Protein 1 - metabolism
Two-Hybrid System Techniques
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Summary: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.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.1215404