Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C

• Published in: FEBS letters 2004-01, Vol.556 (1), p.211-215
• Main Authors: Chitaley, K, Chen, L, Galler, A, Walter, U, Daum, G, Clowes, A.W
• Format: Article
• Language: English
• Subjects: Animals; Aorta - cytology; Cattle; Cell Adhesion Molecules - genetics; Cell Adhesion Molecules - metabolism; Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors; Cyclic AMP-Dependent Protein Kinases - metabolism; Enzyme Inhibitors - pharmacology; Fetal Blood; Focal adhesion; Isoenzymes; Microfilament Proteins; Muscle, Smooth, Vascular - cytology; Myocytes, Smooth Muscle - metabolism; Phosphoproteins - genetics; Phosphoproteins - metabolism; Phosphorylation; Protein Kinase C - antagonists & inhibitors; Protein Kinase C - genetics; Protein Kinase C - metabolism; Rats; Rats, Inbred F344; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Ser/Thr kinase; Serine - metabolism; Serum - physiology; Substrate Specificity
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(03)01435-2

Vasodilator-stimulated phosphoprotein (VASP), an actin binding protein localized to areas of focal contacts, is a substrate for the cyclic adenosine monophosphate/cyclic guanosine monophosphate (cAMP/cGMP)-dependent protein kinases (PKA, PKG). In this study, we show that serum stimulation of vascular smooth muscle cells (SMCs) induces VASP phosphorylation on Ser157, in a mechanism not dependent on PKA or PKG. We tested the possibility that protein kinase C (PKC), a regulator of cytoskeletal function, is involved. PKC inhibition or down-regulation prevented serum-induced phosphorylation of VASP at Ser157 in rat vascular SMCs. Additionally, recombinant PKCα directly phosphorylated Ser157 on VASP. In summary, our data support the hypothesis that PKC phosphorylates VASP and mediates serum-induced VASP regulation.