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UMass Chan Affiliations
Department of Biochemistry and Molecular BiologyGraduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
2008-06-10Keywords
Animals; Endoplasmic Reticulum; Humans; Lectins; Membrane Proteins; Models, Biological; Neoplasm Proteins; Proteasome Endopeptidase Complex; Protein BindingLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
Trends Biochem Sci. 2008 Jul;33(7):298-300. Epub 2008 Jun 4. Link to article on publisher's siteDOI
10.1016/j.tibs.2008.04.013Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32964PubMed ID
18538572Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1016/j.tibs.2008.04.013