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

Research output: Contribution to journalArticlepeer-review

77 Citations (Scopus)

Abstract

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
Volume324
Issue number3
DOIs
Publication statusPublished - 1993 Jun 21
Externally publishedYes

Keywords

  • GLUT1
  • Glucose transporter
  • Glycosylation
  • Subcellular distribution

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'The role of N-glycosylation in the targeting and stability of GLUT1 glucose transporter'. Together they form a unique fingerprint.

Cite this