Molecular Chaperones and Protein Quality Control

Cell. 2006 May 5;125(3):443-51. doi: 10.1016/j.cell.2006.04.014.

Abstract

In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Allosteric Regulation / physiology
  • Animals
  • Cytosol / metabolism
  • Endopeptidase Clp
  • Endoplasmic Reticulum / metabolism
  • HSP70 Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / metabolism
  • Humans
  • Molecular Chaperones / metabolism*
  • Protein Biosynthesis / physiology*
  • Protein Folding*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Protozoan Proteins / metabolism

Substances

  • HSP70 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Proteins
  • Protozoan Proteins
  • Adenosine Triphosphate
  • Endopeptidase Clp
  • ClpB protein, Leishmania