Focus on Membrane Traffic abstract
Nature Cell Biology 1, 330 - 334 (1999)
Published online: 2 September 1999 | doi:10.1038/14020
The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
Christian Appenzeller1,3, Helena Andersson1,3,2, Felix Kappeler1 & Hans-Peter Hauri1
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.
- Department of Pharmacology/Neurobiology, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland
- Present address: Department of Bioscience, NOVUM, S-14157 Huddinge, Sweden
- These authors contributed equally to this work
Correspondence to: Hans-Peter Hauri1 e-mail: Hauri@ubaclu.unibas.ch
