Cooperation of molecular chaperones with the ubiquitin/proteasome system.
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.
Esser
Claudia
C
Institut für Zellbiologie und Bonner Forum Biomedizin, Rheinische Friedrich-Wilhelms-Universität Bonn,Ulrich-Haberland-Str. 61a, D-53121 Bonn, Germany.
Alberti
Simon
S
Höhfeld
Jörg
J
D000818:Animals; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology*; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D017510:Protein Folding; D025801:Ubiquitin / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases / Q000502:physiology
D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D025801:Ubiquitin; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex