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Scientific article
English

Cdc37 goes beyond Hsp90 and kinases

Contributors

MacLean, Morag; Picard, Didier

Published in

Cell stress & chaperones, vol. 8, no. 2, p. 114-119

Publication date

2003

Abstract

Cdc37 is a relatively poorly conserved and yet essential molecular chaperone. It has long been thought to function primarily as an accessory factor for Hsp90, notably directing Hsp90 to kinases as substrates. More recent discoveries challenge this simplistic view. Cdc37 client proteins other than kinases have now been found, and Cdc37 displays a variety of Hsp90-independent activities both in vitro and in vivo. It can function as a molecular chaperone by itself, interact with other Hsp90 cochaperones in the absence of Hsp90, and even support yeast growth and protein folding without its Hsp90-binding domain. Thus, for many substrates, there may be many alternative chaperone pathways involving Cdc37, Hsp90, or both.

Keywords

  • Amino Acid Sequence
  • Animals
  • Cell Cycle Proteins/metabolism
  • Chaperonins
  • Drosophila Proteins
  • HSP90 Heat-Shock Proteins/metabolism
  • Humans
  • Molecular Chaperones/metabolism
  • Molecular Sequence Data
  • Protein Kinases/metabolism
  • Protein Structure, Tertiary
  • Sequence Alignment

Note

The original publication is available at www.springerlink.com

UNIGE affiliation entities

Citation (ISO format)

MACLEAN, Morag, PICARD, Didier. Cdc37 goes beyond Hsp90 and kinases. In: Cell stress & chaperones, 2003, vol. 8, n° 2, p. 114–119. doi: 10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2

Main files (1)

Article (Published version)

Identifiers

Journal ISSN

1355-8145
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Technical informations

Creation

04/12/2009 13:30:00

First validation

04/12/2009 13:30:00

Update

14/03/2023 15:19:28

Status update

14/03/2023 15:19:28

Last indexation

29/10/2024 12:46:56
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