The efficient intracellular sequestration of the insulin-regulatable glucose transporter (GLUT-4) is conferred by the NH2 terminus

• DOI: 10.1083/jcb.117.4.729
• Publication Date: 2004-05-15T00:22:22Z
• Authors: RC Piper; C Tai; JW Slot; CS Hahn; CM Rice; H Huang; DE James
• Keywords: Transport protein

GLUT-4 is the major facilitative glucose transporter isoform in tissues that exhibit insulin-stimulated transport. Insulin regulates transport by rapid translocation of from an intracellular compartment to plasma membrane. A critical feature this process efficient exclusion membrane absence insulin. To identify amino acid domains which confer sequestration, we analyzed subcellular distribution chimeric transporters comprised and a homologous isoform, GLUT-1, found predominantly at cell surface. These were transiently expressed CHO cells using double subgenomic recombinant Sindbis virus vector. We have wild-type targeted morphologically similar observed adipocytes muscle cells. virus-produced GLUT-1 was Substitution amino-terminal region with abolished sequestration GLUT-4. Conversely, substitution NH2 terminus resulted marked GLUT-1. data indicate NH2-terminus both necessary sufficient for sequestration.