From the cradle to the grave: molecular chaperones that may choose between folding and degradation
Public Deposited- Creator
- Hohfeld, J.
- Cyr, D. M.
- Patterson, C.
- 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.
- Date of publication
- 2001
- Keyword
- DOI
- Identifier
- PMCID: PMC1084084
- Onescience id: e752a80628cf82277a26da7471d1840a98e9faa3
- PMID: 11600451
- Publisher DOI: https://doi.org/10.1093/embo-reports/kve206
- Resource type
- Article
- Rights statement
- In Copyright
- Journal title
- EMBO Reports
- Journal volume
- 2
- Journal issue
- 10
- Page start
- 885
- Page end
- 890
- Language
- English
- ISSN
- 1469-3178
- 1469-221X
Relations
- Parents:
This work has no parents.
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