JCB logo
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online
doi:10.1083/jcb.200812121
The Journal of Cell Biology, Vol. 185, No. 5, 827-839
The Rockefeller University Press, 0021-9525 $30.00
© Zhu et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 7758K)
Right arrow PDF+supp data (10896K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Google Scholar
Right arrow Articles by Zhu, Q.
Right arrow Articles by Tsai, R. Y.L.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhu, Q.
Right arrow Articles by Tsai, R. Y.L.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

GNL3L stabilizes the TRF1 complex and promotes mitotic transition



Qubo Zhu, Lingjun Meng, Joseph K. Hsu, Tao Lin, Jun Teishima, and Robert Y.L. Tsai

Center for Cancer and Stem Cell Biology, Alkek Institute of Biosciences and Technology, Texas A&M University System Health Science Center, Houston, TX 77030

Correspondence to Robert Y.L. Tsai: rtsai{at}ibt.tamhsc.edu

Telomeric repeat binding factor 1 (TRF1) is a component of the multiprotein complex "shelterin," which organizes the telomere into a high-order structure. TRF1 knockout embryos suffer from severe growth defects without apparent telomere dysfunction, suggesting an obligatory role for TRF1 in cell cycle control. To date, the mechanism regulating the mitotic increase in TRF1 protein expression and its function in mitosis remains unclear. Here, we identify guanine nucleotide-binding protein-like 3 (GNL3L), a GTP-binding protein most similar to nucleostemin, as a novel TRF1-interacting protein in vivo. GNL3L binds TRF1 in the nucleoplasm and is capable of promoting the homodimerization and telomeric association of TRF1, preventing promyelocytic leukemia body recruitment of telomere-bound TRF1, and stabilizing TRF1 protein by inhibiting its ubiquitylation and binding to FBX4, an E3 ubiquitin ligase for TRF1. Most importantly, the TRF1 protein-stabilizing activity of GNL3L mediates the mitotic increase of TRF1 protein and promotes the metaphase-to-anaphase transition. This work reveals novel aspects of TRF1 modulation by GNL3L.


Q. Zhu and L. Meng contributed equally to this work.

Abbreviations used in this paper: ALT, alternative lengthening of telomeres; APB, ALT-associated PML body; coIP, coimmunoprecipitation; EMSA, electrophoretic mobility shift assay; GNL3L, guanine nucleotide-binding protein-like 3; NS, nucleostemin; PML, promyelocytic leukemia; TRF1, telomeric repeat binding factor 1.

© 2009 Zhu et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents