title: A critical role of heat shock cognate protein 70 in Apoptin-induced phosphorylation of Akt.
abstract: Apoptin, a protein from chicken anemia virus, selectively induces apoptosis of transformed or tumor cells, but not in normal cells. However, the mechanism of action of Apoptin is still not well understood. Using yeast two-hybrid and immunoprecipitation approaches, we found that Apoptin interacted with Heat shock cognate protein 70 (Hsc70). In vivo, Apoptin induced the translocation of endogenous Hsc70 from the cytoplasm to the nucleus, and both were co-localized in the nucleus. In addition, Apoptin induced Akt phosphorylation, which was markedly inhibited by Hsc70 knockdown, suggesting that Hsc70 may play a critical role in Apoptin-induced Akt phosphorylation. These findings help to further understand the molecular mechanism of Apoptin.
authors.affiliation: State Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
authors.forename: Kun
authors.initials: K
authors.lastname: Chen
authors.forename: Zheng
authors.initials: Z
authors.lastname: Luo
authors.forename: Jun
authors.initials: J
authors.lastname: Tang
authors.forename: Shijun J
authors.initials: SJ
authors.lastname: Zheng
mesh_terms: D021581:Active Transport, Cell Nucleus; D017209:Apoptosis; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism*; D055785:Gene Knockdown Techniques; D057809:HEK293 Cells; D050883:HSC70 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D010766:Phosphorylation; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
chemical_list: D036022:Capsid Proteins; D050883:HSC70 Heat-Shock Proteins; C091717:VP3 protein, Chicken anemia virus; D051057:Proto-Oncogene Proteins c-akt