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RESEARCH PRODUCT
Heat Shock Proteins: Cell Protection through Protein Triage
Philippe BonniaudGuillaume WettsteinDavid LanneauCarmen Garridosubject
Proteasome Endopeptidase ComplexHSP27 Heat-Shock Proteinslcsh:MedicinePlasma protein bindingModels Biologicallcsh:TechnologyGeneral Biochemistry Genetics and Molecular Biologycell stressHsp27Heat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock Proteinslcsh:ScienceMini-Review ArticleGeneral Environmental Sciencebiologylcsh:Tubiquitination processlcsh:RGeneral MedicineCrystallinsHsp90Hsp70Cell biologyproteasomeBiochemistryProteasomeheat shock proteinsbiology.proteinlcsh:QSignal transductionProtein qualityProtein BindingSignal Transductiondescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2010-08-10 | The Scientific World Journal |