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Volume 10, Pages 1543-1552
Mini-Review Article

Heat Shock Proteins: Cell Protection through Protein Triage

1INSERM U866, University of Burgundy, Dijon, France
2Faculty of Medicine and Pharmacy, University of Burgundy, Dijon, France
3CHU Dijon, Dijon, France

Received 8 March 2010; Revised 1 June 2010; Accepted 1 July 2010

Academic Editor: Martin Goette

Copyright © 2010 David Lanneau et al.


Heat shock proteins (HSPs) are chaperones that catalyze the proper folding of nascent proteins and the refolding of denatured proteins. The ubiquitin-proteasome system is an error-checking system that directs improperly folded proteins for destruction. A coordinated interaction between the HSPs (renaturation) and the proteasome (degradation) must exist to assure protein quality control mechanisms. Although it still remains unknown how the decision of folding vs. degradation is taken, many pieces of evidence demonstrate that HSPs interact directly or indirectly with the proteasome, assuring quite selectively the proteasomal degradation of certain proteins under stress conditions. In this review, we will describe the different data that demonstrate a role for HSP90, HSP70, HSP27, and alpha-B-crystallin in the partitioning of proteins to either one of these pathways, referred as protein triage.