ASIA unversity:Item 310904400/4618
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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/4618


    Title: Erk associates with and primes GSK-3? for its inactivation resulting in upregulation of ?-catenin
    Authors: Qingqing Ding;Weiya Xia;Jaw-Ching Liu;Jer-Yen Yang;Dung-Fang Lee;Jiahong Xia;Geoffrey Bartholomeusz;Yan Li(Yan Li);Zheng Li;Ralf C. Bargou;Jun Qin;Fuu-Jen Tsai;Chang-Hai Tsai;Mien-Chie Hung
    Date: 2005
    Issue Date: 2009-11-27 13:57:05 (UTC+8)
    Publisher: Asia University
    Abstract: ?-catenin is upregulated in many human cancers and considered to be an oncogene. Hepatocellular carcinoma (HCC) is one of the most prevalent human malignancies, and individuals who are chronic hepatitis B virus (HBV) carriers have a greater than 100-fold increased relative risk of developing HCC. Here we report a mechanism by which HBV-X protein (HBX) upregulates ?-catenin. Erk, which is activated by HBX, associates with GSK-3? through a docking motif (291FKFP) of GSK-3? and phosphorylates GSK-3? at the 43Thr residue, which primes GSK-3? for its subsequent phosphorylation at Ser9 by p90RSK, resulting in inactivation of GSK-3? and upregulation of ?-catenin. This pathway is a general signal, as it was also observed in cell lines in which Erk-primed inactivation of GSK-3? was regulated by IGF-1, TGF-?, and receptor tyrosine kinase HER2, and is further supported by immunohistochemical staining in different human tumors, including cancers of the liver, breast, kidney, and stomach.
    Relation: MOLECULAR CELL 19(2):159-170
    Appears in Collections:[Department of Biotechnology] Journal Article

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