Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding‐defective glycoproteins
- 4 May 2007
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 581 (19) , 3658-3664
- https://doi.org/10.1016/j.febslet.2007.04.070
Abstract
Proteins synthesized in the endoplasmic reticulum (ER) lumen are exposed to several dedicated chaperones and folding factors that ensure efficient maturation. Nevertheless, protein folding remains error-prone and mutations in the polypeptide sequence may significantly reduce folding-efficiency. Folding-incompetent proteins carrying N-glycans are extracted from futile folding cycles in the calnexin chaperone system upon intervention of EDEM1, EDEM2 and EDEM3, three ER-stress-induced members of the glycosyl hydrolase 47 family. This review describes current knowledge about mechanisms regulating folding and disposal of glycoproteins.Keywords
This publication has 63 references indexed in Scilit:
- ERp57 is essential for efficient folding of glycoproteins sharing common structural domainsThe EMBO Journal, 2006
- EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregationBiochemical and Biophysical Research Communications, 2006
- EDEM Is Involved in Retrotranslocation of Ricin from the Endoplasmic Reticulum to the CytosolMolecular Biology of the Cell, 2006
- Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their ActivitiesJournal of Biological Chemistry, 2005
- Energetics of Substrate Binding and Catalysis by Class 1 (Glycosylhydrolase Family 47) α-Mannosidases Involved in N-Glycan Processing and Endoplasmic Reticulum Quality ControlJournal of Biological Chemistry, 2005
- More Than One Glycan Is Needed for ER Glucosidase II to Allow Entry of Glycoproteins into the Calnexin/Calreticulin CycleMolecular Cell, 2005
- The ER protein folding sensor UDP-glucose glycoprotein–glucosyltransferase modifies substrates distant to local changes in glycoprotein conformationNature Structural & Molecular Biology, 2004
- Assembly and Antigen-Presenting Function of MHC Class I Molecules in Cells Lacking the ER Chaperone CalreticulinImmunity, 2002
- XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription FactorCell, 2001
- Setting the Standards: Quality Control in the Secretory PathwayScience, 1999