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MBC in Press, published online ahead of print March 16, 2005
Mol. Biol. Cell 10.1091/mbc.E04-12-1124

A more recent version of this article appeared on June 1, 2005
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Submitted on December 27, 2004
Revised on February 7, 2005
Accepted on March 3, 2005

Insulin-stimulated Plasma Membrane Fusion of Glut4 Glucose Transporter-containing Vesicles Is Regulated by Phospholipase D1

Ping Huang, Yelena M. Altshuller, June Chunqiu Hou, Jeffrey E. Pessin, and Michael A. Frohman

Department of Pharmacology and the Center for Developmental Genetics, University Medical Center at Stony Brook, Stony Brook, NY 11794-5140

Monitoring Editor: Vivek Malhotra

Insulin stimulates glucose uptake in fat and muscle by mobilizing Glut4 glucose transporters from intracellular membrane storage sites to the plasma membrane. This process requires the trafficking of Glut4-containing vesicles toward the cell periphery, docking at exocytic sites, and plasma membrane fusion. We show here that Phospholipase D (PLD) production of the lipid Phosphatidic Acid (PA) is a key event in the fusion process. PLD1 is found on Glut4-containing vesicles, is activated by insulin signaling, and traffics with Glut4 to exocytic sites. Increasing PLD1 activity facilitates glucose uptake whereas decreasing PLD1 activity is inhibitory. Diminished PA production does not substantially hinder trafficking of the vesicles or their docking at the plasma membrane, but does impede fusion-mediated extracellular exposure of the transporter. The fusion block caused by RNAi-mediated PLD1 deficiency is rescued by exogenous provision of a lipid that promotes fusion pore formation and expansion, suggesting that the step regulated by PA is late in the process of vesicle fusion.

Address correspondence to: Michael A. Frohman (michael{at}pharm.sunysb.edu)




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