HSP90 and Co-chaperones: Impact on Tumor Progression and Prospects for Molecular Targeted Cancer TherapyHSP90 inhibitorcancertargeted therapytumor biomarkerclient proteinHeat shock protein 90 (HSP90), a highly and unique chaperone, presents as a double-edged sword. It plays an essential role in ...
The structure of a HOP–TPR–peptide complex explains how TPR domains participate in the assembly of the HSP70–HSP90 multichaperone complex. Article CAS PubMed Google Scholar Schmid, A. B. et al. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. EMBO J. 31, ...
Heat shock protein-90 (Hsp90) is an essential molecular chaperone in eukaryotes involved in maintaining the stability and activity of numerous signalling proteins, also known as clients. Hsp90 ATPase activity is essential for its chaperone function and i
An imbalance between chaperone/co-chaperone levels has been documented in neurons, and suggested to contribute to protein misfolding. An essential protein and a major regulator of protein folding in all eukaryotic cells is the heat shock protein 90 (Hsp90). The function of Hsp90 is tightly ...
Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperonesdoi:10.1007/s00294-014-0432-3Molecular chaperonesHsp90Tetratricopeptide repeat proteinsCo-chaperonesSaccharomyces cerevisiaeThe essential molecular chaperone Hsp90 functions with over ten...
We further show that the co-chaperone Sti1 specifically interacts with and modulates TDP-43 toxicity in a dose-dependent manner. Our study thus uncovers a previously unrecognized tie between Hsp90, Sti1, TDP-43 misfolding, and its cellular toxicity. 展开 ...
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. The Hsp90/Cdc37complex controls the folding of a large proportion of protein kinases and thus stands at the hub of a multitud...
A variety of signaling proteins form heterocomplexes with and are regulated by the heat shock protein chaperone hsp90. These complexes are formed by a multiprotein machinery, including hsp90 and hsp70 as essential and abundant components and Hop, hsp40, and p23 as non-essential cochaperones that...
the HSP90extracellular interactome and suggest that Morgana may regulateHSP90 activity to promote cancer cell migration and suppressantitumor immunity.Signif i cance: This work suggests the potential therapeutic valueof targeting the extracellular HSP90 co-chaperone Morgana toinhibit metastasis formation and...
Hsp90 function can be regulated via cochaperones or post-translational modifications. Inhibition of Hsp90 is an anticancer strategy. Keywords: Hsp90; chaperone; cochaperones; clients; conformational rearrangements; ATPase; post-translational modification 展开 ...