A cyclophilin function in Hsp90-dependent signal transduction
A cyclophilin function in Hsp90-dependent signal transduction
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DOI：
10.1126/science.274.5293.1713
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发表时间：
1996-12-06
期刊：
影响因子：
56.9
通讯作者：
Gaber, RF
中科院分区：
文献类型：
--
作者：
Duina, AA;Chang, HCJ;Gaber, RF
Cpr6和Cpr7是酿酒酵母亲环素-40(CYP-40)的同系物，它们与Hsp90形成复合体，Hsp90是一种在多种信号转导途径中发挥作用的蛋白质伴侣。CPR7的缺失与突变导致Hsp90或Hsp90伴侣机制的另一组分Sti1的数量减少时，会导致严重的生长缺陷。在酵母中表达的两个异源Hsp90依赖的信号转导分子糖皮质激素受体和pp60(v-src)激酶的活性受到cpr7零突变的不利影响。这些结果表明，在正常生长条件下，CYP-40亲环素在Hsp90依赖的信号转导通路中起着普遍的作用。
Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways, Deletion of CPR7 caused severe growth defects when combined with mutations that decrease the amount of Hsp90 or Sti1, another component of the Hsp90 chaperone machinery. The activities of two heterologous Hsp90-dependent signal transducers expressed in yeast, glucocorticoid receptor and pp60(v-src) kinase, were adversely affected by cpr7 null mutations. These results suggest that CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways under normal growth conditions.