کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1930441 1050515 2011 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A critical role of heat shock cognate protein 70 in Apoptin-induced phosphorylation of Akt
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A critical role of heat shock cognate protein 70 in Apoptin-induced phosphorylation of Akt
چکیده انگلیسی

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.


► Apoptin selectively induces apoptosis of transformed or tumor cells.
► We found Apoptin interacted with endogenous Hsc70.
► Apoptin expression induced translocation of Hsc70 from the cytoplasm to the nucleus.
► Knockdown Hsc70 inhibited Apoptin-induced Akt phosphorylation.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 409, Issue 2, 3 June 2011, Pages 200–204
نویسندگان
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