GSBS Student Publications


Sweet bays of ERAD

UMMS Affiliation

Graduate School of Biomedical Sciences; Department of Biochemistry and Molecular Biology



Document Type


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.

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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


Related Resources

Link to Article in PubMed

Journal Title

Trends in biochemical sciences

PubMed ID