Lectins and traffic in the secretory pathway

FEBS Letters

Appenzeller, Christian¹  Kuhn, Franziska¹  Nufer, Oliver¹  Hauri, Hans-Peter¹ 

[1] Department of Pharmacology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

关键词: Calnexin/calreticulin;    Endoplasmic reticulum;    ER–Golgi intermediate compartment;    ERGIC-53;    Golgi;    Lectin;    Mannose 6-phosphate receptor;    Membrane traffic;    Quality control;    VIP36;   

DOI  :  10.1016/S0014-5793(00)01665-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown