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EMBO Rep. 2001 Oct;2(10):885-90.

From the cradle to the grave: molecular chaperones that may choose between folding and degradation.

Author information

  • 1Institut für Zellbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Ulrich-Haberland-Strasse 61a, D-53121 Bonn, Germany. hoehfeld@uni-bonn.de

Abstract

Molecular chaperones are known to facilitate cellular protein folding. They bind non-native proteins and orchestrate the folding process in conjunction with regulatory cofactors that modulate the affinity of the chaperone for its substrate. However, not every attempt to fold a protein is successful and chaperones can direct misfolded proteins to the cellular degradation machinery for destruction. Protein quality control thus appears to involve close cooperation between molecular chaperones and energy-dependent proteases. Molecular mechanisms underlying this interplay have been largely enigmatic so far. Here we present a novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation.

PMID:
11600451
[PubMed - indexed for MEDLINE]
PMCID:
PMC1084084
Free PMC Article

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