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Cdk2: A Genuine Protein Kinase Client of Hsp90 and Cdc37
Biochemistry, 2005Hsp90 and its cochaperone Cdc37 cooperate to provide requisite support to numerous protein kinases involved in cellular signal transduction. In this report, we studied the interactions of Hsp90 and Cdc37 with the cyclin-dependent kinase, Cdk2. Treatment of K562 cells with the Hsp90 inhibitor, geldanamycin, caused a 75% reduction in Cdk2 levels and ...
Thomas, Prince +2 more
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Domain-Mediated Dimerization of the Hsp90 Cochaperones Harc and Cdc37
Biochemistry, 2005Hsp90 is a highly conserved molecular chaperone that acts in concert with Hsp70 and a cohort of cochaperones to mediate the folding of client proteins into functional conformations. The novel Hsp90 cochaperone Harc was identified previously on the basis of its amino acid sequence similarity to Cdc37.
John, Roiniotis +3 more
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Role of Cdc37 in Protein Kinase Folding
2007As nascent chains emerge from the ribosome, they interact with molecular chaperone proteins that prevent aggregation and promote protein folding. Chaperones such as Hsp70 and Hsp40 function together to protect nascent chains while still ribosome bound, and function with little if any specificity for the unfolded polypeptide.
Atin K. Mandal +2 more
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CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone
Molecular and Cellular Biochemistry, 2005Yoshihiko Miyata, Eisuke Nishida
exaly
Cdc37 facilitates cell survival of colorectal carcinoma via activating the CDK4 signaling pathway
Cancer Science, 2018Jianjun Zhu, Fang Yan, Xiaohua Zhu
exaly