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The role of N‐glycosylation in the targeting and stability of GLUT1 glucose transporter
Author(s) -
Asano Tomoichiro,
Takata Kuniaki,
Katagiri Hideki,
Ishihara Hisamitsu,
Inukai Kouichi,
Anai Motonobu,
Hirano Hiroshi,
Yazaki Yoshio,
Oka Yoshitomo
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80129-i
Subject(s) - glut1 , glycosylation , glucose transporter , glucose transporter type 1 , n linked glycosylation , biochemistry , intracellular , transport protein , subcellular localization , biology , chemistry , microbiology and biotechnology , gene , glycoprotein , glycan , endocrinology , insulin
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.