Protein kinase clients are recruited to the Hsp90 molecular chaperone system via Cdc37, which simultaneously binds Hsp90 and kinases and regulates the Hsp90 chaperone cycle. Pharmacological inhibition of Hsp90 in vivo results in degradation of kinase clients, with a therapeutic effect in dependent ...
I. Molecular chaperone machines: chaperone activities of the cyclophilin Cyp-40 and the steroid aporeceptor-associated protein p23. Science 274, 1718–1720 (1996). Article CAS PubMed Google Scholar Roe, S. M. et al. The mechanism of Hsp90 regulation by the protein kinase-specific co...
Many natural products and small molecules have been reported to disrupt protein–protein interactions (PPIs) between Hsp90 and its co-chaperones and client substrates. Such results offer support to the disruption of PPIs as an alternative strategy for selective inhibition of this molecular chaperone. ...
Hsp90 is a highly conserved protein chaperone that interacts with a diverse group of regulatory and signaling proteins including various protein kinases (25, 26, 27), heterotrimeric G proteins (28, 29) and G protein-coupled receptors (30). The functional role of Hsp90 interaction is protein-de...
别名:S cerevisiae hypothetical protein CDC37; CDC 37; CDC37 cell division cycle 37 homolog; CDC37 cell division cycle 37 S cerevisiae homolog; Cdc37 homolog; CDC37 protein; CDC37_HUMAN; CDC37A; Cell division cycle 37 homolog; Hsp90 chaperone protein kinase targeting subunit; Hsp90 chaperone...
The multichaperone heat shock protein (Hsp) 90 complex mediates the maturation and stability of a variety of proteins, many of which are crucial in oncogen
Regulation of Hsp90 ATPase Activity by the Co-chaperone Cdc37p/p50cdc37 Recruitment of protein kinase clients to the Hsp90 complex appears to involve a specialized co-chaperone, Cdc37p/p50(cdc37), whose binding to Hsp90 is... G Siligardi,B Panaretou,P Meyer,... - 《Journal of Biolog...
Heatshockprotein90(HSP90)isamolecularchaperonethatisinducedinresponsetocellularstressandstabilizesclientproteinsinvolvedincellcyclecontrolandproliferative/anti-apoptoticsignalling.Hsp90expressionthatquantityisnormalcellsof2~8times,andmaycontributetotumourcellsurvivalbystabilizingaberrantsignallingproteinsandbyinterferingwith...
Context:Mutations of the RET receptor tyrosine kinase are associated to multiple endocrine neoplasia type 2 (MEN2) and sporadic medullary thyroid carcinoma (MTC). The heat shock protein (HSP) 90 chaperone is required for folding and stability of several kinases. HSP90 is specifically inhibited by...
Kinase Specificity of HSP90 Is Provided by CDC37 To address what determines HSP90 binding at the protein-family level, we analyzed an HSP90 cochaperone, CDC37, known to associate with many kinases (Grammatikakis et al., 1999; Gray et al., 2008). It is not known, however, whether CDC...