Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Am J Physiol Renal Physiol. 2009 Mar;296(3):F459-69. doi: 10.1152/ajprenal.90340.2008. Epub 2008 Oct 29.


Polarized distribution of plasma membrane transporters and receptors in epithelia is essential for vectorial functions of epithelia. This polarity is maintained by sorting of membrane proteins into apical or basolateral transport containers in the trans-Golgi network and/or endosomes followed by their delivery to the appropriate plasma membrane domains. Sorting depends on the recognition of sorting signals in proteins by specific sorting machinery. In the present review, we summarize experimental evidence for and against the hypothesis that N-glycans attached to the membrane proteins can act as apical sorting signals. Furthermore, we discuss the roles of N-glycans in the apical sorting event per se and their contribution to folding and quality control of glycoproteins in the endoplasmic reticulum or retention of glycoproteins in the plasma membrane. Finally, we review existing hypotheses on the mechanism of apical sorting and discuss the potential roles of the lectins, VIP36 and galectin-3, as putative apical sorting receptors.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Endoplasmic Reticulum / metabolism
  • Epithelial Cells / metabolism*
  • Glycoproteins / metabolism*
  • Glycosylation
  • Golgi Apparatus / metabolism
  • Membrane Microdomains / metabolism
  • Membrane Proteins / metabolism*
  • Protein Folding
  • Protein Sorting Signals*
  • Protein Stability


  • Glycoproteins
  • Membrane Proteins
  • Protein Sorting Signals