The lectin ERGIC-53 is a cargo transport receptor for glycoproteins

Abstract

Soluble secretory proteins are transported from the endoplasmic reticulum (ER) to the ER–Golgi intermediate compartment (ERGIC) in vesicles coated with COP-II coat proteins. The sorting of secretory cargo into these vesicles is thought to involve transmembrane cargo-receptor proteins. Here we show that a cathepsin-Z-related glycoprotein binds to the recycling, mannose-specific membrane lectin ERGIC-53. Binding occurs in the ER, is carbohydrate- and calcium-ion-dependent and is affected by untrimmed glucose residues. Binding does not, however, require oligomerization of ERGIC-53, although oligomerization is required for exit of ERGIC-53 from the ER. Dissociation of ERGIC-53 occurs in the ERGIC and is delayed if ERGIC-53 is mislocalized to the ER. These results strongly indicate that ERGIC-53 may function as a receptor facilitating ER-to-ERGIC transport of soluble glycoprotein cargo.

Cite this article

Appenzeller, C., Andersson, H., Kappeler, F. et al. The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat Cell Biol 1, 330–334 (1999). https://doi.org/10.1038/14020

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