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EMBO reports 2, 10, 885–890 (2001)
doi:10.1093/embo-reports/kve206
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Jörg Höhfeld1, Douglas M. Cyr2 & Cam Patterson3
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1 Institut für Zellbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Ulrich-Haberland-Strasse 61a, D-53121 Bonn, Germany
2 Department of Cell and Developmental Biology, School of Medicine, University of North Carolina, Chapel Hill, NC 27599-7090, USA
3 Program in Molecular Cardiology and the Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599-7075, USA
To whom correspondence should be addressed
Jörg Höhfeld Tel: +49 228 735308; Fax: +49 228 735302; hoehfeld@uni-bonn.de
Received 30 May 2001; Accepted 27 August 2001.
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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.
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