Hsp70 is a new target of Sgt1 - an interaction modulated by S100A6
Hsp70 is a new target of Sgt1 - an interaction modulated by S100A6
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DOI：
10.1016/j.bbrc.2007.04.073
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发表时间：
2007-06-15
影响因子：
3.1
通讯作者：
Filipek, Anna
中科院分区：
文献类型：
--
作者：
Splechowicz, Magdalena;Zylicz, Alicja;Filipek, Anna
在这项工作中，我们确定了热休克蛋白70作为一个新的目标的Sgt 1蛋白。使用免疫共沉淀，亲和层析和ELISA，我们表明，除了热休克蛋白90，Sgt 1相互作用的热休克蛋白，热休克蛋白70。我们还发现，Sgt 1的缺失突变体，缺乏的C-末端区域，不结合到热休克蛋白70或热休克蛋白90蛋白。S100 A6是一种与Sgt 1的C-末端部分相互作用的钙结合蛋白，其过表达降低了与Sgt 1结合的伴侣蛋白的量。而在BAPTA/AM处理的细胞中，S100 A6对这种相互作用没有影响，细胞内Ca ~（2+）水平降低。这表明Sgt 1与Hsp 70和Hsp 90的相互作用受S100 A6以Ca 2+依赖的方式调节。(c)2007年爱思唯尔公司All rights reserved.
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. (c) 2007 Elsevier Inc. All rights reserved.