4.5 Review

Lectins and traffic in the secretory pathway

Journal

FEBS LETTERS
Volume 476, Issue 1-2, Pages 32-37

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01665-3

Keywords

calnexin/calreticulin; endoplasmic reticulum; ER-Golgi intermediate compartment; ERGIC-53; Golgi; lectin; mannose 6-phosphate receptor; membrane traffic; quality control; VIP36

Ask authors/readers for more resources

Evidence is accumulating that intracellular animal lectins play important roles in quality control and glycoprotein sorting along the secretory pathway. Calnexin and calreticulin in conjunction with associated chaperones promote correct folding and oligomerization of many glycoproteins in the endoplasmic reticulum (ER), The mannose lectin ERGIC-53 operates as a cargo receptor in transport of glycoproteins from ER to Golgi and the homologous lectin VIP36 may operate in quality control of glycosylation in the Golgi. Exit from the Golgi of lysosomal hydrolases to endosomes requires mannose 6-phosphate receptors and exit to the apical plasma membrane may also involve traffic lectins. Here we discuss the features of these lectins and their role in glycoprotein traffic in the secretory pathway, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available