This Article Full Text Full Text (PDF) Submit a related Letter to the Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints, Permissions and Rights Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Larance, M. Articles by James, D. E. Search for Related Content PubMed PubMed Citation Articles by Larance, M. Articles by James, D. E.

The GLUT4 Code

Diabetes and Obesity Research Program, Garvan Institute of Medical Research, Sydney 2010, Australia

Address all correspondence and requests for reprints to: David E. James, Diabetes and Obesity Research Program, Garvan Institute of Medical Research, Sydney 2010, Australia. E-mail: d.james{at}garvan.org.au.

Despite being one of the first recognized targets of insulin action, the acceleration of glucose transport into muscle and fat tissue remains one of the most enigmatic processes in the insulin action cascade. Glucose transport is accomplished by a shift in the distribution of the insulin-responsive glucose transporter GLUT4 from intracellular compartments to the plasma membrane in the presence of insulin. The complexity in deciphering the molecular blueprint of insulin regulation of glucose transport arises because it represents a convergence of two convoluted biological systems—vesicular transport and signal transduction. Whereas more than 60 molecular players have been implicated in this orchestral performance, it has been difficult to distinguish between mainly passive participants vs. those that are clearly driving the process. The maze-like nature of the endosomal system makes it almost impossible to dissect the anatomical nature of what appears to be a medley of many overlapping and rapidly changing transitions. A major limitation is technology. It is clear that further progress in teasing apart the GLUT4 code will require the development and application of novel and advanced technologies that can discriminate one molecule from another in the living cell and to superimpose this upon a system in which the molecular environment can be carefully manipulated. Many are now taking on this challenge.

This article has been cited by other articles:

				B. Thorens and M. Mueckler Glucose transporters in the 21st Century Am J Physiol Endocrinol Metab, February 1, 2010; 298(2): E141 - E145. [Abstract] [Full Text] [PDF]

				P. Zhao, L. Yang, J. A. Lopez, J. Fan, J. G. Burchfield, L. Bai, W. Hong, T. Xu, and D. E. James Variations in the requirement for v-SNAREs in GLUT4 trafficking in adipocytes J. Cell Sci., October 1, 2009; 122(19): 3472 - 3480. [Abstract] [Full Text] [PDF]

				O. C. Ikonomov, D. Sbrissa, T. Ijuin, T. Takenawa, and A. Shisheva Sac3 Is an Insulin-regulated Phosphatidylinositol 3,5-Bisphosphate Phosphatase: GAIN IN INSULIN RESPONSIVENESS THROUGH Sac3 DOWN-REGULATION IN ADIPOCYTES J. Biol. Chem., September 4, 2009; 284(36): 23961 - 23971. [Abstract] [Full Text] [PDF]

				J. A. Lopez, J. G. Burchfield, D. H. Blair, K. Mele, Y. Ng, P. Vallotton, D. E. James, and W. E. Hughes Identification of a Distal GLUT4 Trafficking Event Controlled by Actin Polymerization Mol. Biol. Cell, September 1, 2009; 20(17): 3918 - 3929. [Abstract] [Full Text] [PDF]

				C. M. Orme and J. S. Bogan Sorting Out Diabetes Science, May 29, 2009; 324(5931): 1155 - 1156. [Abstract] [Full Text] [PDF]

				J. J. Wright, J. Kim, J. Buchanan, S. Boudina, S. Sena, K. Bakirtzi, O. Ilkun, H. A. Theobald, R. C. Cooksey, K. V. Kandror, et al. Mechanisms for increased myocardial fatty acid utilization following short-term high-fat feeding Cardiovasc Res, May 1, 2009; 82(2): 351 - 360. [Abstract] [Full Text] [PDF]

				J. Stockli, J. R. Davey, C. Hohnen-Behrens, A. Xu, D. E. James, and G. Ramm Regulation of Glucose Transporter 4 Translocation by the Rab Guanosine Triphosphatase-Activating Protein AS160/TBC1D4: Role of Phosphorylation and Membrane Association Mol. Endocrinol., December 1, 2008; 22(12): 2703 - 2715. [Abstract] [Full Text] [PDF]

				A. Shisheva Phosphoinositides in insulin action on GLUT4 dynamics: not just PtdIns(3,4,5)P3 Am J Physiol Endocrinol Metab, September 1, 2008; 295(3): E536 - E544. [Abstract] [Full Text] [PDF]

				E. Karnieli and M. Armoni Transcriptional regulation of the insulin-responsive glucose transporter GLUT4 gene: from physiology to pathology Am J Physiol Endocrinol Metab, July 1, 2008; 295(1): E38 - E45. [Abstract] [Full Text] [PDF]