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Originally published In Press as doi:10.1074/jbc.M007610200 on January 12, 2001

J. Biol. Chem., Vol. 276, Issue 14, 10706-10714, April 6, 2001
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Insulin-mediated GLUT4 Translocation Is Dependent on the Microtubule Network*

Ann Louise OlsonDagger , Alan R. Trumbly, and George V. Gibson

From the Department of Biochemistry and Molecular Biology, the University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73190

The GLUT4 facilitative glucose transporter is recruited to the plasma membrane by insulin. This process depends primarily on the exocytosis of a specialized pool of vesicles containing GLUT4 in their membranes. The mechanism of GLUT4 vesicle exocytosis in response to insulin is not understood. To determine whether GLUT4 exocytosis is dependent on intact microtubule network, we measured insulin-mediated GLUT4 exocytosis in 3T3-L1 adipocytes in which the microtubule network was depolymerized by pretreatment with nocodazole. Insulin-mediated GLUT4 translocation was inhibited by more than 80% in nocodazole-treated cells. Phosphorylation of insulin receptor substrate 1 (IRS-1), activation of IRS-1 associated phosphatidylinositide 3-kinase, and phosphorylation of protein kinase B/Akt-1 were not inhibited by nocodazole treatment indicating that the microtubule network was not required for proximal insulin signaling. An intact microtubule network is specifically required for insulin-mediated GLUT4 translocation since nocodazole treatment did not affect insulin-mediated GLUT1 translocation or adipsin secretion. By using in vitro microtubule binding, we demonstrated that both GLUT4 vesicles and IRS-1 bind specifically to microtubules, implicating microtubules in both insulin signaling and GLUT4 translocation. Vesicle binding to microtubules was not mediated through direct binding of GLUT4 or insulin-responsive aminopeptidase to microtubules. A model microtubule-dependent translocation of GLUT4 is proposed.

* This work was supported by Grant DK47894 from the National Institutes of Health and RA0064 from the American Diabetes AssociationThe costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact..

Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, the University of Oklahoma Health Sciences Center, P. O. Box 26901, Rm. 853-BMSB, Oklahoma City, OK 73190. Tel.: 405-271-2227 (ext. 1252); Fax: 405-271-3092; E-mail: ann-olson@ouhsc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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