The role of N-glycosylation in the targeting and stability of GLUT1 glucose transporter

FEBS Lett. 1993 Jun 21;324(3):258-61. doi: 10.1016/0014-5793(93)80129-i.


The cDNAs encoding the GLUT1 glucose transporter protein were altered by site-directed mutagenesis at consensus sites for the addition of N-linked glycosylation. These cDNAs were transfected into CHO cells with an expression vector and the subcellular distribution and stability of the expressed glycosylation-defective GLUT1 protein were analyzed. Immunohistochemical analysis with a specific antibody demonstrated that a significant portion of glycosylation-defective GLUT1 protein remained in the intracellular compartment. By contrast, most of the wild-type GLUT1 protein expressed with the same procedures resided in the plasma membranes. Metabolic labeling studies revealed that the half-life of the glycosylation-defective GLUT1 protein was significantly shorter than that of wild-type GLUT1 protein. These results indicate that N-glycosylation of the glucose transporter affects its intracellular targeting and protein stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • CHO Cells
  • Cricetinae
  • Fluorescent Antibody Technique
  • Glucose Transporter Type 1
  • Glycosylation
  • In Vitro Techniques
  • Monosaccharide Transport Proteins / chemistry
  • Monosaccharide Transport Proteins / metabolism*
  • Mutagenesis, Site-Directed
  • Protein Processing, Post-Translational
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship


  • Glucose Transporter Type 1
  • Monosaccharide Transport Proteins
  • Recombinant Proteins