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J. Biol. Chem., Vol. 269, Issue 20, 14509-14517, 05, 1994
E Butt, K Abel, M Krieger, D Palm, V Hoppe, J Hoppe and U Walter
The vasodilator-stimulated phosphoprotein (VASP) is a major substrate for
cAMP-dependent- (cAK) and cGMP-dependent protein kinase (cGK) in human
platelets and other cardiovascular cells. To identify the VASP
phosphorylation sites, purified VASP was phosphorylated by either protein
kinase and subjected to trypsin, V8 and Lys-C proteolysis. The
phosphorylated proteolytic fragments obtained were separated by reversed
phase high performance liquid chromatography. Sequence analysis of the
phosphorylated peptides and 32P measurement of the released 32P-labeled
amino acids revealed three phosphorylation sites: a serine 1-containing
site (LRKVSKQEEA), a serine 2-containing site (HIERRVSNAG), and a
threonine-containing site (MNAVLARRRKATQVGE). Additional experiments with
purified VASP demonstrated that both cAK and cGK phosphorylated serine 2
rapidly and the threonine residue slowly, whereas cGK phosphorylated the
serine 1 residue more rapidly than the cAK. These differences in the
phosphorylation rates of VASP by the two protein kinases were also observed
with synthetic peptides corresponding to the sequences of the three
identified phosphorylation sites. These experiments also established the
synthetic peptide serine 1 as one of the best in vitro cGK substrates and
the serine 2- containing site as the site responsible for the
phosphorylation-induced mobility shift of VASP in sodium dodecyl
sulfate-polyacrylamide gel electrophoresis. Experiments with 32P-labeled
platelets provided evidence that VASP is phosphorylated at the same three
identified sites also in intact cells and that selective activation of cAK
or cGK primarily increased the phosphorylation of both serine 2 and serine
1 but not threonine. Our results demonstrated overlapping substrate
specificities of cAK and cGK in vitro and in intact cells. However,
important quantitative and qualitative differences between cAK- and cGK-
mediated phosphorylation of the focal adhesion protein VASP in human
platelets were also observed, suggesting distinct functions of the two
types of cyclic nucleotide-mediated VASP phosphorylation.
cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets
Medizinische Universitatsklinik, Klinische Biochemie und Pathobiochemie, Federal Republic of Germany.
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