Exo70 interacts with the Arp2/3 complex and regulates cell migration.
The exocyst is a multiprotein complex essential for tethering secretory vesicles to specific domains of the plasma membrane for exocytosis. Here, we report that the exocyst component Exo70 interacts with the Arp2/3 complex, a key regulator of actin polymerization. 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.
Zuo
Xiaofeng
X
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Zhang
Jian
J
Zhang
Ying
Y
Hsu
Shu-Chan
SC
Zhou
Daoguo
D
Guo
Wei
W
D051376:Actin-Related Protein 2-3 Complex / Q000378:metabolism*; D000818:Animals; D002465:Cell Movement / Q000187:drug effects; D004815:Epidermal Growth Factor / Q000494:pharmacology; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D041681:NIH 3T3 Cells; D011485:Protein Binding / Q000187:drug effects; D051381:Rats; D033921:Vesicular Transport Proteins
D051376:Actin-Related Protein 2-3 Complex; C109901:Exoc7 protein, rat; D008565:Membrane Proteins; D033921:Vesicular Transport Proteins; D004815:Epidermal Growth Factor