Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 33, Issue 7, Pages 298-300Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2008.04.013
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Funding
- NCI NIH HHS [CA79864] Funding Source: Medline
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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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