The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin
Abstract
Terminally misfolded proteins in the endoplasmic reticulum (ER) are retrotranslocated to the cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation (ERAD). EDEM, a postulated Man8B-binding protein, accelerates the degradation of misfolded proteins in the ER. Here, EDEM was shown to interact with calnexin, but not with calreticulin, through its transmembrane region. Both binding of substrates to calnexin and their release from calnexin were required for ERAD to occur. Overexpression of EDEM accelerated ERAD by promoting the release of terminally misfolded proteins from calnexin. Thus, EDEM appeared to function in the ERAD pathway by accepting substrates from calnexin.
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Metadata
- Authors
- Oda, Y., Hosokawa, N., Wada, I., & Nagata, K.
- Venue
- Science
- Published
- 2003-02-28
- Volume
- 299
- Issue
- 5611
- Pages
- 1394-1397
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1984672567
- Cited by
- 453
- References
- 3
- FWCI
- 15.86
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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