Glucose transport activity and ligand binding (cytochalasin B, IAPS-forskolin) of chimeric constructs of GLUT2 and GLUT4 expressed in COS-7-cells

Sonja Wandel, Andreas Buchs, Annette Schürmann, Scott A. Summers, Alvin C. Powers, Michael F. Shanahan, Hans Georg Joost

Research output: Contribution to journalArticlepeer-review

Abstract

Chimeric constructs of glucose transporters GLUT2 and GLUT4 were transiently expressed in COS-7 cells in order to determine regions of the proteins responsible for their differences in activity and ligand binding. Exchange of the C-terminal tail (aa 479-509) of GLUT4 failed to affect glucose transport activity assayed at 1 mM glucose or ligand binding (cytochalasin B, IAPS-forskolin). In contrast, exchange of the C-terminal half of GLUT4 (aa 222-509) for that of GLUT2 markedly reduced ligand binding (K(d)) of cytochalasin B binding 1.88 ± 0.2 μM vs. 0.21 ± 0.06 in the wild-type GLUT4), and moderately (25%) reduced glucose transport activity. These data support the conclusion that the domains determining differences in Ligand binding between GLUT4 and GLUT2 are located in the C-terminal half of the glucose transporters.

Original languageEnglish
Pages (from-to)56-62
Number of pages7
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1284
Issue number1
DOIs
StatePublished - 2 Oct 1996
Externally publishedYes

Keywords

  • 3-[I]Ioda-4-azidophenetylamido-7-O-succinyldeacetyl-forskolin
  • Cytochalasin B
  • Glucose transport
  • Insulin-regulated glucose transporter GLUT4

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