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Cell. 1997 Jan 10;88(1):29-38.

Conformation-independent binding of monoglucosylated ribonuclease B to calnexin.

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1
Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.

Abstract

Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked glycoproteins in vivo. Using defined components, the binding of ribonuclease B (RNase B) Man7-Man9 glycoforms to the luminal domain of calnexin was observed in vitro only if RNase B was monoglucosylated. Binding was independent of the conformation of the glycoprotein. Calnexin protected monoglucosylated RNase B from the action of glucosidase II and PNGase F but not from that of Endo H, which completely released the protein from calnexin. These observations directly demonstrate that calnexin can act exclusively as a lectin.

PMID:
9019402
DOI:
10.1016/s0092-8674(00)81855-3
[Indexed for MEDLINE]
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