Cooperation of molecular chaperones with the ubiquitin/proteasome system

Biochim Biophys Acta. 2004 Nov 29;1695(1-3):171-88. doi: 10.1016/j.bbamcr.2004.09.020.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • HSP70 Heat-Shock Proteins / physiology
  • Humans
  • Molecular Chaperones / physiology*
  • Proteasome Endopeptidase Complex / physiology*
  • Protein Folding
  • Ubiquitin / physiology*
  • Ubiquitin-Protein Ligases / physiology


  • HSP70 Heat-Shock Proteins
  • Molecular Chaperones
  • Ubiquitin
  • STUB1 protein, human
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex