| Title | Cooperation of molecular chaperones with the ubiquitin/proteasome system. | | Author(s) | Esser C, Alberti S, Höhfeld J | | Institution | Institut für Zellbiologie und Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn,Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany. | | Source | Biochim Biophys Acta 2004 Nov 29; 1695(1-3):171-88. | | MeSH | Animals
HSP70 Heat-Shock Proteins
Humans
Molecular Chaperones
Proteasome Endopeptidase Complex
Protein Folding
Research Support, Non-U.S. Gov't
Ubiquitin
Ubiquitin-Protein Ligases
| | Abstract | Molecular chaperones and energy-dependent proteases have long been viewed as opposing forces that control protein biogenesis. Molecular chaperones are specialized in protein folding, whereas energy-dependent proteases such as the proteasome mediate efficient protein degradation. Recent data, however, suggest that molecular chaperones directly cooperate with the ubiquitin/proteasome system during protein quality control in eukaryotic cells. Modulating the intracellular balance of protein folding and protein degradation may open new strategies for the treatment of human diseases that involve chaperone pathways such as cancer and diverse amyloid diseases. | | Language | eng | | Pub Type(s) | Journal Article
Review
| | PubMed ID | 15571814 |
|
