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This version published online on November 6, 2003
Molecular Endocrinology, doi:10.1210/me.2003-0089
Molecular Endocrinology Vol. 0, No. 2003 200300891-
doi:10.1210/me.2003-0089
Copyright © 2003 by the Endocrine Society.
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Submitted on March 18, 2003
Accepted on October 30, 2003

Carboxy Terminus of Glucose Transporter GLUT3 Contains an Apical Membrane Targeting Domain

Kouichi Inukai1, Annette M. Shewan1, Wendy S. Pascoe1, Shigehiro Katayama1, David E. James1, and Yoshitomo Oka1*

1 Fourth Department of Internal Medicine, Saitama Medical School, 350-0495, Japan and Division of Molecular Metabolism and Diabetes, Department of Internal Medicine Tohoku University Graduate School of Medicine, 980-8574, Japan and Institute for Molecular Bioscience, University of Queensland, Brisbane, 4072, Australia and Garvan Institute of Medical Research, St Vincents Hospital, Sydney, 2010, Australia

* To whom correspondence should be addressed. E-mail: oka{at}int3.med.tohoku.ac.jp.

We previously demonstrated that distinct facilitative glucose transporter isoforms display differential sorting in polarized epithelial cells. In MDCK cells, GLUT1 and GLUT2 are localized to the basolateral cell surface while GLUTs 3 and 5 are targeted to the apical membrane (Pascoe et al. Am. J. Physiol. 271, C547-554, 1996). To explore the molecular mechanisms underlying this asymmetric distribution, we analyzed the targeting of chimeric glucose transporter proteins in MDCK cells. Replacement of the carboxy terminal cytosolic tail of GLUT1, GLUT2 or GLUT4 with that from GLUT3 resulted in apical targeting. Conversely, a GLUT3 chimera containing the cytosolic carboxy terminus of GLUT2 was sorted to the basolateral membrane. These findings are not attributable to the presence of a basolateral signal in the tails of GLUTs 1, 2 and 4 because the basolateral targeting of GLUT1 was retained in a GLUT1 chimera containing the carboxy terminus of GLUT5. In addition, we were unable to demonstrate the presence of an autonomous basolateral sorting signal in the GLUT1 tail using the LDL receptor as a reporter. By examining the targeting of a series of more defined GLUT1/3 chimeras, we found evidence of an apical targeting signal involving residues 473-484 (DRSGKDGVMEMN) in the carboxy tail. We conclude that the targeting of GLUT3 to the apical cell surface in MDCK cells is regulated by a unique cytosolic sorting motif.




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