The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest
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DOI：
10.1016/s0014-5793(00)01134-0
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发表时间：
2000-02-04
期刊：
影响因子：
3.5
通讯作者：
Picard, D
中科院分区：
文献类型：
--
作者：
Abbas-Terki, T;Donzé, O;Picard, D
分子伴侣Cdc 37被认为部分作为热休克蛋白90（Hsp 90）伴侣复合物的靶向亚基。我们在这里证明，Cdc 37所需的激酶Ste 11在芽殖酵母的活性。cdc 37突变株在Ste 11介导的信息素信号传导以及组成型活性Ste 11版本Ste 11 Delta N的积累和功能成熟方面存在缺陷。此外，Cdc 37、Ste 11 Delta N和Hsp 90成对共沉淀。因此，热休克蛋白90和Cdc 37可以短暂地与Ste 11相关，以促进正确的折叠和/或与其他调控因子的关联。我们的研究结果建立Ste 11作为第一个内源性Cdc 37客户蛋白在酵母。(C)2000年欧洲生物化学学会联合会。
The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast. A cdc37 mutant strain is defective in Ste11-mediated pheromone signaling and in accumulation and functional maturation of the constitutively active Ste11 version Ste11 Delta N. Moreover, Cdc37, Ste11 Delta N and Hsp90 coprecipitate pairwise. Thus, Hsp90 and Cdc37 may transiently associate with Ste11 to promote proper folding and/or association with additional regulatory factors. Our results establish Ste11 as the first endogenous Cdc37 client protein in yeast. (C) 2000 Federation of European Biochemical Societies.