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Lectins and traffic in the secretory pathway
Author(s) -
Hauri Hans-Peter,
Appenzeller Christian,
Kuhn Franziska,
Nufer Oliver
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01665-3
Subject(s) - calnexin , golgi apparatus , endoplasmic reticulum , endosome , microbiology and biotechnology , secretory pathway , glycoprotein , calreticulin , glycosylation , lectin , glycan , mannose , transport protein , chemistry , biology , biochemistry , intracellular
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.