Pathways of chaperone-mediated protein folding in the cytosol

Nat Rev Mol Cell Biol. 2004 Oct;5(10):781-91. doi: 10.1038/nrm1492.


Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many proteins, the folding process requires the action of molecular chaperones. In the cytosol of prokaryotic and eukaryotic cells, molecular chaperones of different structural classes form a network of pathways that can handle substrate polypeptides from the point of initial synthesis on ribosomes to the final stages of folding.

Publication types

  • Review

MeSH terms

  • Animals
  • Bacterial Proteins / metabolism
  • Chaperonins / metabolism
  • Cytoplasm / metabolism*
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / metabolism
  • Models, Biological
  • Molecular Chaperones / metabolism*
  • Protein Conformation
  • Protein Folding*
  • Protein Transport
  • Ribosomes / metabolism


  • Bacterial Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Chaperonins