A proteomic snapshot of the human heat shock protein 90 interactome
A proteomic snapshot of the human heat shock protein 90 interactome
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DOI：
10.1016/j.febslet.2005.10.020
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发表时间：
2005-11-21
期刊：
影响因子：
3.5
通讯作者：
Kungl, AJ
中科院分区：
文献类型：
--
作者：
Falsone, SF;Gesslbauer, B;Kungl, AJ
热休克蛋白90（Hsp90）是一种分子伴侣，可调节细胞内的几种信号通路。通过应用免疫共沉淀与内源性热休克蛋白90，我们能够确定39个新的蛋白质相互作用的伴侣，这种伴侣在人胚肾细胞（HEK293）。有趣的是，DNA活化蛋白激酶催化亚基，在这项研究中发现的热休克蛋白90相互作用的合作伙伴，被发现是敏感的Hsp90抑制剂治疗，只有在HeLa细胞，但不是在HEK293细胞指的是这种伴侣的致瘤性。(c)2005年欧洲生物化学学会联合会。Elsevier B.V.出版，保留所有权利。
Heat shock protein 90 (Hsp90) is a molecular chaperone which modulates several signalling pathways within a cell. By applying co-immunoprecipitation with endogeneous Hsp90, we were able to identify 39 novel protein interaction partners of this chaperone in human embryonic kidney cells (HEK293). Interestingly, levels of DNA-activated protein kinase catalytic subunit, an Hsp90 interaction partner found in this study, were found to be sensitive to Hsp90 inhibitor treatment only in HeLa cells but not in HEK293 cells referring to the tumorgenicity of this chaperone. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.