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Nature Structural Biology  10, 319 - 321 (2003)
doi:10.1038/nsb0503-319

EDEM an ER quality control receptor

Tao Wang & Daniel N. Hebert

Tao Wang and Daniel N. Hebert are in the Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts 01003, USA.

Correspondence should be addressed to Daniel N. Hebert dhebert@biochem.umass.edu
Defective proteins in the endoplasmic reticulum (ER) are tagged as terminally aberrant by the composition of their N-linked glycans. The ER carbohydrate-binding protein EDEM selectively recognizes such tags and sorts the defective proteins for degradation via the ERAD pathway.

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REFERENCE
Glycoproteins
Nature Encyclopaedia of Life Sciences

REVIEWS
Quality control in the endoplasmic reticulum
Nature Reviews Molecular Cell Biology Review (01 Mar 2003)

NEWS AND VIEWS
Recognizing misfolded proteins in the endoplasmic reticulum
Nature Structural Biology News and Views (01 Apr 2000)
Insights into checkpoint capacity
Nature Structural & Molecular Biology News and Views (01 Feb 2004)

RESEARCH
Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
The EMBO Journal Article (01 Dec 1999)
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
Nature Cell Biology Article (01 Oct 1999)
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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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