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.
MeSH Terms
Carrier Proteins/metabolism
Cloning, Molecular
Fluorescent Antibody Technique
HeLa Cells
Humans
Intracellular Signaling Peptides and Proteins
Mass Spectrometry
RNA Interference
Shelterin Complex
Telomere/metabolism,physiology
Telomere-Binding Proteins/metabolism
Telomeric Repeat Binding Protein 1/metabolism
Two-Hybrid System Techniques
Chemicals
Carrier Proteins
Intracellular Signaling Peptides and Proteins
PAK1IP1 protein, human
POT1 protein, human
Shelterin Complex
TINF2 protein, human
Telomere-Binding Proteins
Telomeric Repeat Binding Protein 1
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Ye Jeffrey Zheng-Sheng
Laboratory for Cell Biology and Genetics and Laboratory for Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, New York 10021, USA.
[email protected]
Hockemeyer Dirk
Krutchinsky Andrew N
Loayza Diego
Hooper Sarah M
Chait Brian T
de Lange Titia
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