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• W3166412030 abstract "Protein kinases are important regulators in cellular signal transduction. As one major type of Hsp90 client, protein kinases rely on the ATP-dependent molecular chaperone Hsp90, which maintains their structure and supports their activation. Depending on client type, Hsp90 interacts with different cofactors. Here we report that besides the kinase-specific cofactor Cdc37 large PPIases of the Fkbp-type strongly bind to kinase•Hsp90•Cdc37 complexes. We evaluate the nucleotide regulation of these assemblies and identify prominent interaction sites in this quaternary complex. The synergistic interaction between the participating proteins and the conserved nature of the interaction suggests functions of the large PPIases Fkbp51/Fkbp52 and their nematode homolog FKB-6 as contributing factors to the kinase cycle of the Hsp90 machinery." @default.
• W3166412030 created "2021-06-22" @default.
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• W3166412030 date "2021-06-11" @default.
• W3166412030 modified "2023-10-06" @default.
• W3166412030 title "HSP-90/kinase complexes are stabilized by the large PPIase FKB-6" @default.
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• W3166412030 doi "https://doi.org/10.1038/s41598-021-91667-5" @default.
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