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From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Author(s) -
Höhfeld Jörg,
Cyr Douglas M,
Patterson Cam
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve206
Subject(s) - co chaperone , chaperone (clinical) , protein folding , foldase , proteases , hsp90 , microbiology and biotechnology , protein quality , biology , biochemistry , proteostasis , protein degradation , chemistry , computational biology , heat shock protein , enzyme , groel , gene , medicine , pathology , escherichia coli
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.