The ubiquitylation machinery of the endoplasmic reticulum

Nature. 2009 Mar 26;458(7237):453-60. doi: 10.1038/nature07962.


As proteins travel through the endoplasmic reticulum (ER), a quality-control system retains newly synthesized polypeptides and supports their maturation. Only properly folded proteins are released to their designated destinations. Proteins that cannot mature are left to accumulate, impairing the function of the ER. To maintain homeostasis, the protein-quality-control system singles out aberrant polypeptides and delivers them to the cytosol, where they are destroyed by the proteasome. The importance of this pathway is evident from the growing list of pathologies associated with quality-control defects in the ER.

Publication types

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

MeSH terms

  • Animals
  • Endoplasmic Reticulum / chemistry
  • Endoplasmic Reticulum / metabolism*
  • Homeostasis
  • Humans
  • Intracellular Membranes / metabolism
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Folding
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Ubiquitination*


  • Proteins
  • Proteasome Endopeptidase Complex