Closing in on the Hsp90 chaperone-client relationship

Klaus Richter; Johannes Buchner

doi:10.1016/j.str.2011.03.007

Closing in on the Hsp90 chaperone-client relationship

Klaus Richter, Johannes Buchner

Research output: Contribution to journal › Short survey › peer-review

11 Scopus citations

Abstract

The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

Original language	English
Pages (from-to)	445-446
Number of pages	2
Journal	Structure
Volume	19
Issue number	4
DOIs	https://doi.org/10.1016/j.str.2011.03.007
State	Published - 13 Apr 2011

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title = "Closing in on the Hsp90 chaperone-client relationship",

abstract = "The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.",

author = "Klaus Richter and Johannes Buchner",

note = "Funding Information: Work in the authors' labs was supported by grants from the DFG, the BMBF, and the Fonds der chemischen Industrie. The authors thank Jing Li for help with the artwork, and Marco Retzlaff for stimulating discussions.",

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AU - Richter, Klaus

AU - Buchner, Johannes

N1 - Funding Information: Work in the authors' labs was supported by grants from the DFG, the BMBF, and the Fonds der chemischen Industrie. The authors thank Jing Li for help with the artwork, and Marco Retzlaff for stimulating discussions.

PY - 2011/4/13

Y1 - 2011/4/13

N2 - The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

AB - The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

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DO - 10.1016/j.str.2011.03.007

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SN - 0969-2126

VL - 19

SP - 445

EP - 446

JO - Structure

JF - Structure

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Closing in on the Hsp90 chaperone-client relationship

Abstract

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