Appenzeller, C. and Andersson, H. and Kappeler, F. and Hauri, H. P.. (1999) The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nature Cell Biology, Vol. 1, H. 6. pp. 330-334.
Full text not available from this repository.
Official URL: http://edoc.unibas.ch/dok/A5257769
Downloads: Statistics Overview
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.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Pharmacology/Neurobiology (Hauri) |
---|---|
UniBasel Contributors: | Hauri, Hans-Peter |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | MacMillan |
ISSN: | 1465-7392 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Last Modified: | 25 Mar 2014 13:05 |
Deposited On: | 22 Mar 2012 14:13 |
Repository Staff Only: item control page