The endoplasmic reticulum-associated degradation and disulfide reductase ERdj5

Methods Enzymol. 2011;490:235-58. doi: 10.1016/B978-0-12-385114-7.00014-3.


The endoplasmic reticulum (ER) is an organelle where secretory or membrane proteins are correctly folded with the aid of various molecular chaperones and oxidoreductases. Only correctly folded and assembled proteins are enabled to reach their final destinations, which are called as ER quality control (ERQC) mechanisms. ER-associated degradation (ERAD) is one of the ERQC mechanisms for maintaining the ER homeostasis and facilitates the elimination of misfolded or malfolded proteins accumulated in the ER. ERAD is mainly consisting of three processes: recognition of misfolded proteins for degradation in the ER, retrotranslocation of (possibly) unfolded substrates from the ER to the cytosol through dislocation channel, and their degradation in the cytosol via ubiquitin-protesome system. After briefly mentioned on productive folding of nascent polypeptides in the ER, we here overview the above three processes in ERAD system by highlighting on novel ERAD factors such as EDEM and ERdj5 in mammals and yeasts.

MeSH terms

  • Animals
  • Disulfides / metabolism
  • Endoplasmic Reticulum / enzymology*
  • Endoplasmic Reticulum / physiology
  • Glycosylation
  • HSP40 Heat-Shock Proteins / genetics
  • HSP40 Heat-Shock Proteins / metabolism*
  • Humans
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Protein Folding
  • Proteins / chemistry
  • Proteins / metabolism
  • Stress, Physiological / physiology
  • Ubiquitin / metabolism
  • Unfolded Protein Response / physiology


  • DNAJC10 protein, human
  • Disulfides
  • HSP40 Heat-Shock Proteins
  • Molecular Chaperones
  • Proteins
  • Ubiquitin