Hsp90 reaches new heights

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Abstract
The first international meeting on the Hsp90 (heat‐shock protein 90) chaperone machine was held in Arolla, Switzerland, from 24 to 28 August 2002. Located in a beautiful isolated chalet, high in the Swiss Alps, this was a highly interactive and productive gathering, whose success owed much to its organizers, Didier Picard and Johannes Buchner. ![][1] Hsp90 (heat‐shock protein 90) is an abundant molecular chaperone, but its function seems to be restricted to the folding of proteins involved in cell signalling, such as transcription factors and protein kinases. This restricted set of ‘clients’ (see Fig. 1) makes Hsp90 an attractive target for cancer therapeutics. As an anti‐Hsp90 drug is now in clinical trials, the meeting was relevant to a broad range of scientists interested in its chaperone activity. However, even with this clinical relevance, a meeting devoted to just one chaperone might seem like too much of a good thing, unless one takes into account the myriad of co‐chaperones that regulate Hsp90. These co‐chaperones modulate the ATPase activity of Hsp90 and many of them have intrinsic chaperone activity of their own, providing some measure of specificity for different Hsp90 clients. There is also some crossover between different chaperone machineries, as some co‐chaperones interact with Hsp70 as well as Hsp90. Figure 1. Examples of roles of Hsp90 and its co‐chaperones in different cellular processes through their interactions with different client proteins. The conference was opened by D. Smith (Scottsdale, AZ, USA), who gave a historical perspective on the interactions of Hsp90 and its co‐chaperones with steroid receptors (reviewed by Pratt & Toft, 1997). His presentation began with a review of the work of Toft and Gorksi from the late 1960s, in which an oestrogen receptor was identified and found to exist in a large complex of proteins. Smith followed the identification and characterization of Hsp90 … [1]: pending:yes