EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin

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Science  28 Feb 2003:
Vol. 299, Issue 5611, pp. 1394-1397
DOI: 10.1126/science.1079181

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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.

  • * Present address: Institute of Biomedical Sciences, Fukushima Medical University, Fukushima 960–1295, Japan.

  • To whom correspondence should be addressed. E-mail: nagata{at}

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