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PMID: 14627196 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Cdc37 goes beyond Hsp90 and kinases.

Cell stress & chaperones ·Vol. 8 ·No. 2 ·2003-00-00 ·Pages 114-9

MacLean M, Picard D

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.

MeSH Terms
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
Chemicals
CDC37 protein, human Cell Cycle Proteins Drosophila Proteins HSP90 Heat-Shock Proteins Molecular Chaperones Protein Kinases Chaperonins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
MacLean Morag
Département de Biologie Cellulaire, Université de Genève, Sciences III, 30, quai Ernest-Ansermet, CH-1211 Genève 4, Switzerland.
Picard Didier
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Article Info
Journal
Cell stress & chaperones
Abbr.
Cell Stress Chaperones
ISSN
1355-8145
DOI
10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2
Published
2003-00-00
Pages
114-9
Language
English
Region
Netherlands
NLM ID
9610925
PMCID
PMC514862
Subset
IM
External Links
PubMed source DOI: 10.1379/1466-1268(2003)008<0114:cgbhak>2.0.co;2 PMC Full Text View journal details
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