A role for endocytosis and exocytosis in cell migration has been proposed but not yet demonstrated. Here we show that cellubrevin, an early endosomal v-SNARE, mediates trafficking in the lamellipod of migrating epithelial cells and partially colocalizes with markers of focal contacts. Expression of tetanus neurotoxin, which selectively cleaves cellubrevin, significantly reduced the speed of migrating epithelial cells. Furthermore, expression of tetanus neurotoxin enhanced the adhesion of epithelial cells to collagen, laminin, fibronectin and E-cadherin, altered spreading on collagen, and impaired the recycling of ?1 integrins. These results suggest that cellubrevin-dependent membrane trafficking participates in cell motility through the regulation of cell adhesion
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