2017
DOI: 10.1038/nrm.2017.20
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The HSP90 chaperone machinery

Abstract: The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis under both physiological and stress conditions in eukaryotic cells. As HSP90 has several hundred protein substrates (or 'clients'), it is involved in many cellular processes beyond protein folding, which include DNA repair, development, the immune response and neurodegenerative disease. A large number of co-chaperones interact with HSP90 and regulate the ATPase-associated conformational changes of the HSP90 dimer that occu… Show more

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Cited by 1,209 publications
(1,302 citation statements)
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References 201 publications
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“…Extensive data on HSP90 are compiled on public databases such as phosphosite.org which listed, as of 4th of May 2017 no less than 168 PTMs sites for HSP90β and 179 for HSP90α. The main PTMs known on HSP90 have been reviewed in detail before, together with their functional significance, when known [6,21,44,7782]. Rather, here, we will cover the few studies assessing the impact of HSP90 inhibition on the global proteome PTMs (Figure 2).…”
Section: Global Impact Of Hsp90 Inhibition On the Proteomementioning
confidence: 99%
See 1 more Smart Citation
“…Extensive data on HSP90 are compiled on public databases such as phosphosite.org which listed, as of 4th of May 2017 no less than 168 PTMs sites for HSP90β and 179 for HSP90α. The main PTMs known on HSP90 have been reviewed in detail before, together with their functional significance, when known [6,21,44,7782]. Rather, here, we will cover the few studies assessing the impact of HSP90 inhibition on the global proteome PTMs (Figure 2).…”
Section: Global Impact Of Hsp90 Inhibition On the Proteomementioning
confidence: 99%
“…Its folding activity is connected with a complex ATP-driven cycle characterized by large conformational changes, which correlate with binding and dissociation of interactors [5]. HSP90 interactors are classified in three major categories: other chaperones, co-chaperones and cofactors, and clients [6]. Clients form the most diverse and numerous categories of interactors.…”
Section: Introductionmentioning
confidence: 99%
“…AhR forms a complex with the molecular chaperone HSP90, co-chaperone p23, and the hepatitis B virus X-associated protein XAP2 in the cytoplasm [14] [15] [16]. The molecular chaperone HSP90 regulates the physiological functions of more than 300 proteins including the steroid hormone receptors in the cells [1] [2]. We reported the activation mechanisms of AHR by HSP90 [9].…”
Section: Discussionmentioning
confidence: 99%
“…The relative orientation of domains in AIPL1 might be important for proper positioning of AIPL1 and HSP90 with respect to the PDE6 catalytic dimer during the enzyme assembly. HSP90 functions as a dimer [62, 63], and its two TPR-acceptor sites, in theory, could be simultaneously occupied by two molecules of AIPL1 that would act on the two catalytic subunits of the PDE6 dimer. This hypothetical chaperone-client complex would require a precise alignment of PDE6-AIPL1 and PDE6-HSP90 interaction surfaces.…”
Section: Role Of the Aipl1 Tpr Domainmentioning
confidence: 99%