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MBC in Press, published online ahead of print July 26, 2006
Mol. Biol. Cell 10.1091/mbc.E06-04-0278

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Submitted on April 6, 2006
Revised on June 27, 2006
Accepted on July 18, 2006

Role of Insulin-dependent Cortical Fodrin/Spectrin Remodeling in GLUT4 Translocation in Rat Adipocytes

Libin Liu,* Mark P. Jedrychowski,* Steven P. Gygi,{dagger} and Paul F. Pilch*

*Department of Biochemistry, Boston University Medical School, Boston, MA 02118; {dagger}Department of Cell Biology, Harvard Medical School, Boston, MA 02115

Monitoring Editor: Robert Parton

Fodrin or nonerythroid spectrin is an abundant component of the cortical cytoskeletal network in rat adipocytes. Fodrin has a highly punctate distribution in resting cells and insulin causes a dramatic remodeling of fodrin to a more diffuse pattern. Insulin-mediated remodeling of actin occurs to a lesser extent than does that of fodrin. We show that fodrin interacts with the t-SNARE syntaxin 4, and this interaction is increased by insulin stimulation and decreased by prior Latrunculin A treatment. Latrunculin A disrupts all actin filaments, inhibits GLUT4 translocation, and causes fodrin to partially redistribute from the plasma membrane to the cytosol. In contrast, Cytochalasin D disrupts only the short actin filament signal, and Cytochalasin D neither inhibits GLUT4 translocation nor fodrin redistribution in adipocytes. Taken together, our data suggest that insulin induces remodeling of the fodrin-actin network, which is required for the fusion of GLUT4 storage vesicles (GSVs) with the plasma membrane by permitting their access to the t-SNARE syntaxin 4.

Address correspondence to: Paul F. Pilch (ppilch{at}bu.edu)




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