Get 20M+ Full-Text Papers For Less Than $1.50/day. Subscribe now for You or Your Team.

Learn More →

PTOP interacts with POT1 and regulates its localization to telomeres

PTOP interacts with POT1 and regulates its localization to telomeres Telomere maintenance has been implicated in cancer and ageing, and requires cooperation between a multitude of telomeric factors, including telomerase, TRF1, TRF2, RAP1, TIN2, Tankyrase, PINX1 and POT1 (refs 1–12). POT1 belongs to a family of oligonucleotide-binding (OB)-fold-containing proteins that include Oxytricha nova TEBP, Cdc13, and spPot1, which specifically recognize telomeric single-stranded DNA (ssDNA) 10,13,14,15,16,17,18,19 . In human cells, the loading of POT1 to telomeric ssDNA controls telomerase-mediated telomere elongation 12 . Surprisingly, a human POT1 mutant lacking an OB fold is still recruited to telomeres. However, the exact mechanism by which this recruitment occurs remains unclear. Here we identify a novel telomere protein, PTOP, which interacts with both POT1 and TIN2. PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres. Inhibition of PTOP by RNA interference (RNAi) or disruption of the PTOP–POT1 interaction hindered the localization of POT1 to telomeres. Furthermore, expression of the respective interaction domains on PTOP and POT1 alone extended telomere length in human cells. Therefore, PTOP heterodimerizes with POT1 and regulates POT1 telomeric recruitment and telomere length. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Cell Biology Springer Journals

PTOP interacts with POT1 and regulates its localization to telomeres

Loading next page...
 
/lp/springer-journals/ptop-interacts-with-pot1-and-regulates-its-localization-to-telomeres-ApA00XNugz

References (31)

Publisher
Springer Journals
Copyright
Copyright © 2004 by Nature Publishing Group
Subject
Life Sciences; Life Sciences, general; Cell Biology; Cancer Research; Developmental Biology; Stem Cells
ISSN
1465-7392
eISSN
1476-4679
DOI
10.1038/ncb1142
Publisher site
See Article on Publisher Site

Abstract

Telomere maintenance has been implicated in cancer and ageing, and requires cooperation between a multitude of telomeric factors, including telomerase, TRF1, TRF2, RAP1, TIN2, Tankyrase, PINX1 and POT1 (refs 1–12). POT1 belongs to a family of oligonucleotide-binding (OB)-fold-containing proteins that include Oxytricha nova TEBP, Cdc13, and spPot1, which specifically recognize telomeric single-stranded DNA (ssDNA) 10,13,14,15,16,17,18,19 . In human cells, the loading of POT1 to telomeric ssDNA controls telomerase-mediated telomere elongation 12 . Surprisingly, a human POT1 mutant lacking an OB fold is still recruited to telomeres. However, the exact mechanism by which this recruitment occurs remains unclear. Here we identify a novel telomere protein, PTOP, which interacts with both POT1 and TIN2. PTOP binds to the carboxyl terminus of POT1 and recruits it to telomeres. Inhibition of PTOP by RNA interference (RNAi) or disruption of the PTOP–POT1 interaction hindered the localization of POT1 to telomeres. Furthermore, expression of the respective interaction domains on PTOP and POT1 alone extended telomere length in human cells. Therefore, PTOP heterodimerizes with POT1 and regulates POT1 telomeric recruitment and telomere length.

Journal

Nature Cell BiologySpringer Journals

Published: Jun 6, 2004

There are no references for this article.