Abstract
Vascular endothelial growth factor receptor-2 (VEGFR-2) plays a key role in vasculogenesis and pathophysiological angiogenesis. The mechanism of secretory transport and delivery of VEGFR-2 to the plasma membrane is poorly understood. In the present study, using human umbilical vein endothelial cells (HUVECs) we demonstrate that post-Golgi trafficking of VEGFR-2 is regulated by syntaxin 6, a t-SNARE involved in membrane fusion events along the secretory pathway. Inhibition of syntaxin 6 function using recombinant adenoviruses expressing cytosolic inhibitory forms significantly reduces cell surface VEGFR-2 (but not transferrin receptor) and blocks post-Golgi transport of HA-tagged VEGFR-2 (but not VSV-G). Inhibitory forms of syntaxins 8, or 12 had no effect on cell surface levels or post-Golgi trafficking of HA-tagged VEGFR-2. VEGFR-2 and syntaxin 6 co-localize at Golgi apparatus and co-immunoprecipitate. HUVECs expressing inhibitory forms of syntaxin 6 completely blocked VEGF-induced HUVECs proliferation and migration. Together our data support a model in which syntaxin 6 regulate delivery of VEGFR-2 from the Golgi apparatus to the cell surface thereby regulating VEGF-induced cell migration and proliferation.
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