English  |  正體中文  |  简体中文  |  Items with full text/Total items : 90451/105768 (86%)
Visitors : 11067827      Online Users : 627
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version


    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/4573


    Title: GSK-3? targets Cdc25A for ubiquitin-mediated proteolysis and GSK-3? inactivation leads to Cdc25A overproduction in human cancers
    Authors: Kang, T.;Wei, Y.;Honaker, Y.;Yamaguchi, H.;Appella, E.;Mien-Chie Hung;Piwnica-Worms, H.
    Keywords: CELLCYCLE;SIGNALING
    Date: 2008
    Issue Date: 2009-11-27 13:56:53 (UTC+8)
    Publisher: Asia University
    Abstract: The Cdc25A phosphatase positively regulates cell-cycle transitions, is degraded by the proteosome throughout interphase and in response to stress, and is overproduced in human cancers. The kinases targeting Cdc25A for proteolysis during early cell-cycle phases have not been identified, and mechanistic insight into the cause of Cdc25A overproduction in human cancers is lacking. Here, we demonstrate that glycogen synthase kinase-3beta (GSK-3beta) phosphorylates Cdc25A to promote its proteolysis in early cell-cycle phases. Phosphorylation by GSK-3beta requires priming of Cdc25A, and this can be catalyzed by polo-like kinase 3 (Plk-3). Importantly, a strong correlation between Cdc25A overproduction and GSK-3beta inactivation was observed in human tumor tissues, indicating that GSK-3beta inactivation may account for Cdc25A overproduction in a subset of human tumors.
    Relation: CANCER CELL 13(-):36-47
    Appears in Collections:[生物科技學系] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML238View/Open


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


    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback