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• W2100215915 abstract "•Hsp90 recognises substrate by an extended interface with scattered hydrophobics. •Hsp90 binds folded proteins, folding intermediates, and disordered proteins. •Binding specificity determines that Hsp70 acts early and Hsp90 acts late. The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how Hsp90 achieves client specificity and its role in the cellular chaperone cascade. Interestingly, Hsp90 has an extended substrate binding interface that crosses domain boundaries, exhibiting specificity for proteins with hydrophobic residues spread over a large area regardless of whether they are disordered, partly folded, or even folded. This specificity principle ensures that clients preferentially bind to Hsp70 early on in the folding path, but downstream folding intermediates bind Hsp90. Discussed here, the emerging model is that the Hsp90 ATPase does not modulate client affinity but instead controls substrate influx from Hsp70. The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how Hsp90 achieves client specificity and its role in the cellular chaperone cascade. Interestingly, Hsp90 has an extended substrate binding interface that crosses domain boundaries, exhibiting specificity for proteins with hydrophobic residues spread over a large area regardless of whether they are disordered, partly folded, or even folded. This specificity principle ensures that clients preferentially bind to Hsp70 early on in the folding path, but downstream folding intermediates bind Hsp90. Discussed here, the emerging model is that the Hsp90 ATPase does not modulate client affinity but instead controls substrate influx from Hsp70. the Hsp90 co-chaperone that stimulates the ATP hydrolysis rate. Aha1 binds to Hsp90-N and Hsp90-M and competes with p23. a kinase-specific substrate targeting factor of Hsp90. The human homologue is known as p50. cyclin-dependent kinase 4 requires Hsp90 to reach the active state, like many other kinases. an E3 ubiquitin ligase, specifically interacts with both Hsp70 and Hsp90. It specifically targets the TPR motifs at the C terminus of the chaperone by its TPR domain and ubiquitylates chaperone-bound clients. Hsp90 substrates are also known as clients. In this review, we use both terms synonymously. single-particle electron microscopy provides structural information on protein complexes by constructing 3D models of biomolecules from 2D electron micrographs. In cryo-EM, particles are studied at cryogenic temperatures in their native states, whereas negative staining techniques involve the use of heavy metal salts, which interact with the electron beam and produce phase contrast. ‘Hsp’ stands for heat shock protein, ‘90’ for an apparent molecular weight of 90 kDa. The predominant homologue in the human cytosol is the constitutive Hsp90β, while Hsp90α is heat inducible. Thus, Hsp90β is not a heat shock protein, and it is 83 kDa. nuclear magnetic resonance provides a dynamic picture of molecules and protein complexes in solution, based on signals of nuclei that have a particular label. the Hsp90 co-chaperone that slows down ATP hydrolysis. p23 binds to both N-terminal domains and Hsp90-M and competes with Aha1. p23 binding induces N-terminal dimerisation of Hsp90. ‘proteostasis’ is an acronym for protein homeostasis. It involves all maintenance processes from protein synthesis to protein degradation. In particular, molecular chaperones and proteases control proteostasis; together they form the proteostasis network. small angle X-ray scattering, a solution method that provides a distance distribution curve between the atoms of a molecule. The distance distribution allows one to calculate structural models in solutions if further data are available, e.g., from crystallographic or NMR studies. a tetratricopeptide motif is a specific recognition site at the C terminus of a protein. Recognition typically involves the carboxy group of the last residue, thus several TPR binding proteins need to compete for the same site." @default.
• W2100215915 created "2016-06-24" @default.
• W2100215915 creator A5075205750 @default.
• W2100215915 creator A5078715883 @default.
• W2100215915 date "2015-02-01" @default.
• W2100215915 modified "2023-10-14" @default.
• W2100215915 title "Hsp90 interaction with clients" @default.
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• W2100215915 doi "https://doi.org/10.1016/j.tibs.2014.12.002" @default.
• W2100215915 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25579468" @default.
• W2100215915 hasPublicationYear "2015" @default.
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