CDC37型
伴侣(临床)
热休克蛋白90
细胞生物学
激酶
生物
蛋白质折叠
共同伴侣
细胞内
信号转导
热休克蛋白
蛋白激酶A
生物化学
医学
基因
细胞外信号调节激酶
病理
作者
Thomas L. Prince,Benjamin Lang,Yuka Okusha,Takanori Eguchi,Stuart K. Calderwood
出处
期刊:Sub-cellular biochemistry
日期:2022-12-16
卷期号:: 141-158
被引量:7
标识
DOI:10.1007/978-3-031-14740-1_5
摘要
The co-chaperone p50/Cdc37 is an important partner for Hsp90, assisting in molecular chaperone activities, particularly with regard to the regulation of protein kinases. Analysis of the structure of Hsp90-Cdc37-kinase complexes demonstrates the way in which Cdc37 interacts with and controls the folding of a large proportion of intracellular protein kinases. This co-chaperone thus stands at the hub of a multitude of intracellular signaling networks. Indeed, the influence of Cdc37 reaches beyond the housekeeping pathways of protein folding into the regulation of a wide range of cellular processes. This co-chaperone has attracted attention as a potential intermediate in carcinogenesis. Cdc37 is an attractive potential target in cancer due to (1) high expression in a number of tumor types and (2) control of multiple signaling pathways. These properties indicate (3) a potential for selectivity due to its elevated expression in malignant cells and (4) robustness, as the co-chaperone may control multiple growth signaling pathways and thus be less prone to evolution of resistance than less versatile oncoproteins. Cdc37 may also be involved in other aspects of pathophysiology and has been shown to be secreted in exosomes. Protein aggregation disorders have been linked to age-related declines in molecular chaperones and co-chaperones. Cdc37 also appears to be a potential agent in longevity due to its links to protein folding and autophagy, and it will be informative to study the role of Cdc37 maintenance/decline in aging organisms.
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