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Papers In Press, published online ahead of print November 1, 2001
J. Biol. Chem, 10.1074/jbc.M108280200
Submitted on August 28, 2001
Revised on October 30, 2001
Accepted on October 31, 2001

A PI 3-kinase independent insulin signaling pathway to N-WASP/Arp2-3/F-actin required for GLUT4 glucose transporter recycling

Zhen Y. Jiang, Anil Chawla, Avirup Bose, Michael Way, and Michael P. Czech

Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605

Corresponding Author: Michael.Czech{at}umassmed.edu

Recruitment of intracellular glucose transporter 4 (GLUT4) to the plasma membrane of fat and muscle cells in response to insulin requires phosphatidylinositol (PI) 3-kinase as well as a proposed PI 3-kinase independent pathway leading to activation of the small GTPase TC10. Here we show that in cultured adipocytes insulin causes acute cortical localization of the actin-regulatory neural Wiskott-Aldrich syndrome protein (N-WASP) and actin-related protein-3 (Arp3) as well as cortical F-actin polymerization by a mechanism that is insensitive to the PI 3-kinase inhibitor wortmannin. Expression of the dominant inhibitory N-WASP-deltaWA protein lacking the Arp and actin binding regions attenuates the cortical F-actin rearrangements by insulin in these cells. Remarkably, the N-WASP-deltaWA protein also inhibits insulin action on GLUT4 translocation, indicating dependence of GLUT4 recycling on N-WASP- directed cortical F-actin assembly. TC10 exhibits sequence similarity to cdc42, and has been reported to bind N-WASP. We show the inhibitory TC10 (T31N) mutant, which abrogates insulin-stimulated GLUT4 translocation and glucose transport, also inhibits both cortical localization of N-WASP and F-actin formation in response to insulin. These findings reveal that N-WASP likely functions downstream of TC10 in a PI 3-kinase-independent insulin signaling pathway to mobilize cortical F-actin, which in turn promotes GLUT4 responsiveness to insulin.


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