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• W1971496338 abstract "The facilitative glucose transporter 1 (GLUT1) mediates the passive diffusion of d-glucose across the cell membrane, providing the energy resource in glycolysis in the erythrocytes. Anion exchanger 1 (band 3) is another important membrane protein that mediates rapid exchange of CO(2) through Cl(-)/HCO(3)(-) exchange across the erythrocyte membrane. For verifying the presumption over a decade that GLUT1 and band 3 in the erythrocyte would be interacting with each other, we cloned and expressed both the cytoplasmic domains of GLUT1 and band 3 in Escherichia coli, and tested their binding ability. By coimmunoprecipitation we found that among the tested N-terminal, C-terminal, and loop fraction of GLUT1, only the C-terminal of GLUT1 can interact with cytoplasmic domain of band 3. The interaction was further verified by coimmunoprecipitation and pull-down assay using both proteins as bait and target. These results showed that GLUT1 and band 3 form a protein complex that can regulate the activities of the proteins within it." @default.
• W1971496338 created "2016-06-24" @default.
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• W1971496338 date "2006-01-01" @default.
• W1971496338 modified "2023-10-16" @default.
• W1971496338 title "Interaction of glucose transporter 1 with anion exchanger 1 in vitro" @default.
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• W1971496338 doi "https://doi.org/10.1016/j.bbrc.2005.11.138" @default.
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• W1971496338 hasPublicationYear "2006" @default.
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