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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/86895

    Title: De-acetylation and degradation of HSPA5 is critical for E1A metastasis suppression in breast cancer cells
    Authors: Chang, YW;Chang, YW;Chen, HA;Chen, HA;Tseng, CF;Tseng, CF;Hong, CC;Hong, CC;Ma, JT;Ma, JT;Hung, MC;Hung, MC;Wu, CH;Wu, CH;Huang, MT;Huang, MT;蘇振良*
    Contributors: 生物科技學系
    Date: 2014-10
    Issue Date: 2014-11-07 14:47:10 (UTC+8)
    Abstract: Elevated expression of heat shock protein 5 (HSPA5) promotes drug resistance and metastasis and is a marker of poor prognosis in breast cancer patients. Adenovirus type 5 E1A gene therapy has demonstrated antitumor efficacy but the mechanisms of metastasis-inhibition are unclear. Here, we report that E1A interacts with p300 histone acetyltransferase (HAT) and blocks p300-mediated HSPA5 acetylation at K353, which in turn promotes HSPA5 ubiquitination by GP78 (E3 ubiquitin ligase) and subsequent proteasome-mediated degradation. Our findings point out the Ying-Yang regulation of two different post-translational modifications (ubiquitination and acetylation) of HSPA5 in tumor metastasis.
    Relation: Oncotarget;5(21):10558-70.
    Appears in Collections:[生物科技學系] 期刊論文

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