English  |  正體中文  |  简体中文  |  Items with full text/Total items : 28588/40619
Visitors : 4201363      Online Users : 60
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45502

Title: PP2A and ​Aurora differentially modify ​Cdc13 to promote telomerase release from telomeres at G2/M phase.
Authors: Zih-Jie Shen;Pang-Hung Hsu;Yu-Tai Su;Chia-Wei Yang;Li Kao;Shun-Fu Tseng;Ming-Daw Tsai;Shu-Chun Teng
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2014
Issue Date: 2018-03-22T02:42:59Z
Publisher: Nature Communications
Abstract: Abstract: In yeast, the initiation of telomere replication at the late S phase involves in combined actions of kinases on Cdc13, the telomere binding protein. Cdc13 recruits telomerase to telomeres through its interaction with Est1, a component of telomerase. However, how cells terminate the function of telomerase at G2/M is still elusive. Here we show that the protein phosphatase 2A (PP2A) subunit Pph22 and the yeast Aurora kinase homologue Ipl1 coordinately inhibit telomerase at G2/M by dephosphorylating and phosphorylating the telomerase recruitment domain of Cdc13, respectively. While Pph22 removes Tel1/Mec1-mediated Cdc13 phosphorylation to reduce Cdc13–Est1 interaction, Ipl1-dependent Cdc13 phosphorylation elicits dissociation of Est1–TLC1, the template RNA component of telomerase. Failure of these regulations prevents telomerase from departing telomeres, causing perturbed telomere lengthening and prolonged M phase. Together our results demonstrate that differential and additive actions of PP2A and Aurora on Cdc13 limit telomerase action by removing active telomerase from telomeres at G2/M phase.
Relation: 5
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45502
Appears in Collections:[生命科學系] 期刊論文

Files in This Item:

File Description SizeFormat

All items in NTOUR are protected by copyright, with all rights reserved.


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback