ERAD: The Long Road to Destruction

Nat Cell Biol. 2005 Aug;7(8):766-72. doi: 10.1038/ncb0805-766.

Abstract

Endoplasmic reticulum (ER)-associated protein degradation (ERAD) eliminates misfolded or unassembled proteins from the ER. ERAD targets are selected by a quality control system within the ER lumen and are ultimately destroyed by the cytoplasmic ubiquitin-proteasome system (UPS). The spatial separation between substrate selection and degradation in ERAD requires substrate transport from the ER to the cytoplasm by a process termed dislocation. In this review, we will summarize advances in various aspects of ERAD and discuss new findings on how substrate dislocation is achieved.

Publication types

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

MeSH terms

  • Animals
  • Endoplasmic Reticulum / metabolism*
  • Humans
  • Membrane Transport Proteins / metabolism
  • Models, Biological
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Folding
  • Protein Transport
  • Proteins / chemistry
  • Proteins / metabolism
  • Ubiquitin / metabolism
  • Ubiquitin-Protein Ligase Complexes / metabolism*
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / metabolism
  • Ubiquitin-Protein Ligases / physiology
  • Yeasts / metabolism

Substances

  • Membrane Transport Proteins
  • Proteins
  • Ubiquitin
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases
  • Proteasome Endopeptidase Complex