Sweet bays of ERAD
Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Biology
Medical Subject Headings
Animals; Endoplasmic Reticulum; Humans; Lectins; Membrane Proteins; Models, Biological; Neoplasm Proteins; Proteasome Endopeptidase Complex; Protein Binding
Life Sciences | Medicine and Health Sciences
Proteins that improperly mature in the endoplasmic reticulum (ER) are dislocated to the cytoplasm for proteasome-mediated destruction. A recent study provides insight into the incompletely understood processes for selection and targeting of aberrant proteins for ER-associated protein degradation. The identification of the ER chaperones GRP94 and BiP as binding partners for the mannose-binding proteins OS-9 and XTP3-B, indicates that these protein complexes bind to aberrant proteins and direct them to the Hrd1 dislocation and ubiquitylation complex in the ER membrane.
Rights and Permissions
Citation: Trends Biochem Sci. 2008 Jul;33(7):298-300. Epub 2008 Jun 4. Link to article on publisher's site
DOI of Published Version
Trends in biochemical sciences
Tamura, Taku; Cormier, James H.; and Hebert, Daniel N., "Sweet bays of ERAD" (2008). GSBS Student Publications. 1515.