Abstract
Enabled/Vasodilator-stimulated phosphoprotein (Ena/VASP) protein family members link actin dynamics and cellular signaling pathways. VASP localizes to regions of dynamic actin reorganization such as the focal adhesion contacts, the leading edge or filopodia, where it contributes to F-actin filament elongation. Here we identify VASP as a novel substrate for protein kinase D1 (PKD1). We show that PKD1 directly phosphorylates VASP at two serine residues, Ser-157 and Ser-322. These phosphorylations occur in response to RhoA activation and mediate VASP re-localization from focal contacts to the leading edge region. The net result of this PKD1-mediated phosphorylation switch in VASP is increased filopodia formation and length at the leading edge. However, such signaling when persistent induced membrane ruffling and decreased cell motility.
Highlights
Protein kinase D1 (PKD1) regulates actin reorganization processes at the leading edge
We found that in presence of active PKD1, vasodilator-stimulated phosphoprotein (VASP) shows increased phosphorylation as well as an electrophoretic mobility shift from 46 to 50 kDa (Fig. 1A), which previously was described to be due to phosphorylation at Ser-157, but not Ser-239 and Thr-278 [2, 14]
Protein kinase D1 interacts with F-actin and regulates actin reorganization at several levels [22]
Summary
Protein kinase D1 (PKD1) regulates actin reorganization processes at the leading edge. We show that PKD1 directly phosphorylates VASP at two serine residues, Ser-157 and Ser-322 These phosphorylations occur in response to RhoA activation and mediate VASP re-localization from focal contacts to the leading edge region. The net result of this PKD1-mediated phosphorylation switch in VASP is increased filopodia formation and length at the leading edge Such signaling when persistent induced membrane ruffling and decreased cell motility. We show that PKD1 phosphorylates VASP at two serine residues, Ser-157 and Ser-322 in the EVH-2 domain These phosphorylations occur in response to RhoA activation and mediate VASP translocation from focal contacts to the leading edge region. PKD1-mediated phosphorylation of VASP increases stress fiber formation resulting in increased lamellipodium formation and filopodia length When persistent such signaling resulted in membrane ruffling and decreased cell migration
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
