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Vasodilator‐stimulated phosphoprotein is a substrate for protein kinase C
Author(s) -
Chitaley K,
Chen L,
Galler A,
Walter U,
Daum G,
Clowes A.W
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01435-2
Subject(s) - phosphoprotein , protein kinase c , phosphorylation , protein kinase a , microbiology and biotechnology , cyclic guanosine monophosphate , cgmp dependent protein kinase , cyclic adenosine monophosphate , kinase , chemistry , adcy6 , adenosine , guanosine , mitogen activated protein kinase kinase , biochemistry , biology , receptor , camp dependent pathway , nitric oxide , organic chemistry
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.