Lectins and traffic in the secretory pathway

FEBS Lett. 2000 Jun 30;476(1-2):32-7. doi: 10.1016/s0014-5793(00)01665-3.


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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Binding Proteins / metabolism*
  • Calnexin
  • Calreticulin
  • Glycoproteins / metabolism*
  • Humans
  • Lectins / chemistry
  • Lectins / metabolism*
  • Molecular Chaperones / metabolism
  • Protein Folding
  • Ribonucleoproteins / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • Calcium-Binding Proteins
  • Calreticulin
  • Glycoproteins
  • Lectins
  • Molecular Chaperones
  • Ribonucleoproteins
  • Calnexin