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J. Biol. Chem., Vol. 269, Issue 4, 2353-2356, 01, 1994
KJ Verhey and MJ Birnbaum
In the insulin-responsive tissues, muscle and adipose, the GLUT4 glucose
transporter isoform accounts for most of the increase in hexose flux in
response to hormone. In these cell types, as well as in fibroblasts
transfected with cDNAs encoding the transporters, GLUT1 and GLUT4 are
sorted to different subcellular locations. In the latter, GLUT1 is found
primarily at the cell surface whereas GLUT4 localizes to the interior of
the cell in a perinuclear distribution. The construction and analysis of
chimeras of these two transporter isoforms have allowed identification of
the COOH-terminal 30 amino acids as a critical sorting signal for
differential localization of the transporters. In this study, we show that
2 residues present in the GLUT4 COOH terminus, Leu-489 and Leu-490, are
critical for the intracellular sequestration of this isoform in NIH3T3
cells.
A Leu-Leu sequence is essential for COOH-terminal targeting signal of GLUT4 glucose transporter in fibroblasts
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
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