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Papers In Press, published online ahead of print September 8, 2005
Molecular Transport, Garvan Institute of Medical Research, Darlinghurst, N.S.W. 2010
Corresponding Author: d.james{at}garvan.org.au
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 in order to discover potential regulators of GLUT4 trafficking. In addition to previously identified components of GLUT4 storage vesicles including the insulin regulated aminopeptidase IRAP, and the v-SNARE VAMP2, we have identified three new rab proteins: rab10, rab11, and rab14 on GLUT4 vesicles. We have also found that the putative rabGAP AS160 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 IRAP, 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 shRNA 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.
J. Biol. Chem, 10.1074/jbc.M503897200
Submitted on April 11, 2005
Revised on August 31, 2005
Accepted on September 8, 2005
Characterisation of the role of the RabGAP AS160 in insulin-regulated GLUT4 trafficking
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