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

Tomoichiro Asano, Kuniaki Takata, Hideki Katagiri, Hisamitsu Ishihara, Kouichi Inukai, Motonobu Anai, Hiroshi Hirano, Yoshio Yazaki, Yoshitomo Oka

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81 Citations (Scopus)


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 proteins 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.

Original languageEnglish
Pages (from-to)258-261
Number of pages4
JournalFEBS Letters
Issue number3
Publication statusPublished - 1993 Jun 21


  • GLUT1
  • Glucose transporter
  • Glycosylation
  • Subcellular distribution


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