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J. Biol. Chem., Vol. 280, Issue 45, 37803-37813, November 11, 2005

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Characterization of the Role of the Rab GTPase-activating Protein AS160 in Insulin-regulated GLUT4 Trafficking^*

Mark Larance1, Georg Ramm1, Jacqueline Stöckli12, Ellen M. van Dam, Stephanie Winata, Valerie Wasinger, Fiona Simpson¶, Michael Graham||, Jagath R. Junutula**, Michael Guilhaus, and David E. James, A National Health and Medical Research Council senior principal research fellow3

From the Diabetes and Obesity Program, Garvan Institute of Medical Research, Sydney 2010, Australia, Bioanalytical Mass Spectrometry Facility, University of New South Wales, Sydney 2052, Australia, ^¶Institute for Molecular Biology, University of Queensland, Brisbane 4072, Australia, ^||Benitec, Inc., Mountain View, California 94043, and ^**Genentech Inc., South San Francisco, California 94080

Insulin stimulates the translocation of the glucose transporter GLUT4 from intracellular vesicles to the plasma membrane. In the present study we have conducted a comprehensive proteomic analysis of affinity-purified GLUT4 vesicles from 3T3-L1 adipocytes to discover potential regulators of GLUT4 trafficking. In addition to previously identified components of GLUT4 storage vesicles including the insulin-regulated aminopeptidase insulin-regulated aminopeptidase and the vesicle soluble N-ethylmaleimide factor attachment protein (v-SNARE) VAMP2, we have identified three new Rab proteins, Rab10, Rab11, and Rab14, on GLUT4 vesicles. We have also found that the putative Rab GTPase-activating protein AS160 (Akt substrate of 160 kDa) is associated with GLUT4 vesicles in the basal state and dissociates in response to insulin. This association is likely to be mediated by the cytosolic tail of insulin-regulated aminopeptidase, which interacted both in vitro and in vivo with AS160. Consistent with an inhibitory role of AS160 in the basal state, reduced expression of AS160 in adipocytes using short hairpin RNA increased plasma membrane levels of GLUT4 in an insulin-independent manner. These findings support an important role for AS160 in the insulin regulated trafficking of GLUT4.

Received for publication, April 11, 2005 , and in revised form, August 31, 2005.

^* This work was supported in part by grants from the National Health and Medical Research Council of Australia and Diabetes Australia Research Trust (to D. E. J.). Mass spectrometric analysis for this work was carried out at the Bioanalytical Mass Spectrometry Facility, University of New South Wales, and was supported in part by grants from the Australian Government Systemic Infrastructure Initiative and Major National Research Facilities Program (University of New South Wales node of the Australian Proteome Analysis Facility) and by the University of New South Wales Capital Grants Scheme. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table 2.

¹ These authors contributed equally to this work.

² Supported by the Swiss National Foundation and the Novartis Stiftung.

³ To whom correspondence should be addressed: Diabetes and Obesity Program, Garvan Institute of Medical Research, 384 Victoria St., Darlinghurst, NSW 2010 Australia. Tel.: 61-2-92958210; Fax: 61-2-92958201; E-mail: d.james{at}garvan.org.au.

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