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. 2009 Jan;16(1):2-6.
doi: 10.1038/nsmb0109-2.

The Hsp90 mosaic: a picture emerges

Matthias P Mayer  1 , Chrisostomos Prodromou, Judith Frydman
Affiliations

The Hsp90 mosaic: a picture emerges

Matthias P Mayer et al. Nat Struct Mol Biol. 2009 Jan.

Abstract

Hsp90s, molecular chaperones critically involved in many essential cellular processes, were the focus of a recent international conference held in Seeon, Germany. The scope of the conference ranged from structural and mechanistic insights all the way to medical applications.

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Figures

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Figure 1 The ATPase cycle of Hsp90 proteins. Model of the ATPase cycle of Hsp90 proteins as revealed by kinetic analysis of ATP binding and/or conformational changes of yeast cytosolic Hsp82, human endoplasmic reticulum GRP94, human mitochondrial TRAP1 and E. coli HtpG. Hsp90 proteins proceed through two distinct intermediates before reaching the γ-phosphate cleavage–competent conformation. Forward and backward reaction rates are different for the individual Hsp90 proteins analyzed and may be subjected to regulation by cochaperones such as Aha1. A proposed compact post-hydrolysis state visible in EM seems to be transient and is not detectable by bulk measurements like SAXS or HX-MS.
Figure 2
Figure 2
A cycle of phosphorylation and dephosphorylation of Cdc37 is necessary for kinase-client loading onto Hsp90. Cdc37, phosphorylated by CK2, binds to kinases and forms a complex with Hsp90. The PP5 (also known as Ppt1) phosphatase binds to the C terminus of Hsp90 and dephosphorylates Cdc37, which subsequently dissociates from the Hsp90 complex. ATP binding and hydrolysis by Hsp90 and interaction with additional cochaperones lead to maturation and release of the kinase.[Au: e.g. instead of i.e. meant for Aha1?]
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