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    Please use this identifier to cite or link to this item: https://ir.fy.edu.tw:8080/ir/handle/987654321/7106


    Title: The viral death protein Apoptin interacts with Hippi, the protein interactor of Huntingtin-interacting protein 1.
    Authors: Chih-Mei Cheng;Shiao-ping Huang;Yung-Fu Chang;Wen-Yuan Chung;Chung-Yee Yuo
    Contributors: 輔英科技大學 醫學檢驗生物技術系
    Keywords: Apoptin;Hippi;Hip-1;Death effector domain;Apoptosis;Tumor-specific apoptotic activity
    Date: 2003-04-01
    Issue Date: 2010-10-15 16:05:31 (UTC+8)
    Abstract: Apoptin, a chicken anemia virus-encoded protein, induces apoptosis in human tumor cells but not in normal cells. The tumor-specific activity of Apoptin is correlated with its nuclear localization in tumor cells. In an attempt to elucidate the molecular mechanism of Apoptin-induced apoptosis, we identified human Hippi, the protein interactor and apoptosis co-mediator of Huntingtin interacting protein 1, as one of the Apoptin-associated proteins by yeast two-hybrid screen. We also demonstrated that Hippi could interact with Apoptin both in vitro and in human cells. Furthermore, subcellular localization studies showed that Hippi and Apoptin perfectly colocalized in the cytoplasm of normal human HEL cells, whereas in cancerous HeLa cells most Apoptin and Hippi were located separately in the nucleus and cytoplasm and, thus, showed only a modest colocalization. Mapping studies indicate that Hippi binds within the self-multimerization domain of Apoptin, and Apoptin binds to the C-terminal half of Hippi, including its death effector domain-like motif. Our results suggest that the Apoptin–Hippi interaction may play a role in the suppression of apoptosis in normal cells.
    Relation: Biochemical and Biophysical Research Communications 305(2),359-364
    Appears in Collections:[醫學檢驗生物技術系] 期刊論文

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