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Volume 154, Issue 2
23 July 2001
Journal of Cell Biology Cover Image for Volume 154, Issue 2
Article Contents
Review| July 23 2001

Hsp90 : a specialized but essential protein-folding tool

Jason C. Young,
Jason C. Young
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
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Ismail Moarefi,
Ismail Moarefi
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
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F. Ulrich Hartl
F. Ulrich Hartl
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
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Author and Article Information
Jason C. Young
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
Ismail Moarefi
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
F. Ulrich Hartl
Cellular Biochemistry, Max Planck Institute for Biochemistry, Martinsried D-82152, Germany
Address correspondence to Ulrich Hartl, Dept. of Cellular Biochemistry, Max-Planck-Institut für Biochemie, Am Kopferspitz 18a, Martinsried D-82152, Germany. Tel.: 49-89-8578-2233. Fax: 49-89-8578-2211. E-mail: [email protected]
*

Abbreviations used in this paper: AMP-PNP, 5′-adenylylimidodiphosphate; GA, geldanamycin; HSF, heat shock transcription factor; TPR, tetratricopeptide repeat.

Received: April 19 2001
Revision Received: June 14 2001
Accepted: June 21 2001
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2001
J Cell Biol (2001) 154 (2): 267–274.
https://doi.org/10.1083/jcb.200104079
Article history
Received:
April 19 2001
Revision Received:
June 14 2001
Accepted:
June 21 2001

Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy.

The Rockefeller University Press
2001
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