کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1937991 | 1050729 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Hsp70 is a new target of Sgt1—an interaction modulated by S100A6
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In this work, we identified Hsp70 as a novel target of the Sgt1 protein. Using co-immunoprecipitation, affinity chromatography and ELISA we showed that, besides Hsp90, Sgt1 interacts with the heat shock protein, Hsp70. We also found that a deletion mutant of Sgt1, devoid of the C-terminal region, did not bind to either Hsp70 or Hsp90 proteins. Overexpression of S100A6, a calcium binding protein that interacts with the C-terminal part of Sgt1, decreased the amount of chaperone bound to Sgt1. However, the effect of S100A6 on this interaction was not observed in BAPTA/AM treated cells in which Ca2+ level was decreased. This suggests that the interaction of Sgt1 with Hsp70 and Hsp90 is regulated by S100A6 in a Ca2+-dependent manner.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 4, 15 June 2007, Pages 1148–1153
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 4, 15 June 2007, Pages 1148–1153
نویسندگان
Magdalena Spiechowicz, Alicja Zylicz, Paweł Bieganowski, Jacek Kuznicki, Anna Filipek,