Journal
NATURE CELL BIOLOGY
Volume 8, Issue 12, Pages 1383-U38Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1505
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The exocyst is a multiprotein complex essential for tethering secretory vesicles to specific domains of the plasma membrane for exocytosis(1-3). Here, we report that the exocyst component Exo70 interacts with the Arp2/3 complex, a key regulator of actin polymerization(4,5). We further show that the exocyst Arp2/3 interaction is regulated by epidermal growth factor (EGF) signalling. Inhibition of Exo70 by RNA interference (RNAi) or antibody microinjection blocks the formation of actin-based membrane protrusions and affects various aspects of cell motility. We propose that Exo70, in addition to functioning in exocytosis, also regulates actin at the leading edges of migrating cells, therefore coordinating cytoskeleton and membrane traffic during cell migration.
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