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J. Biol. Chem., Vol. 275, Issue 40, 30817-30825, October 6, 2000
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From the Department of Cell Biology, Zoological Institute,
Technical University of Braunschweig,
D-38092 Braunschweig, Germany
The vasodilator-stimulated phosphoprotein (VASP)
is a major substrate for cyclic nucleotide-dependent
kinases in platelets and other cardiovascular cells. It promotes actin
nucleation and binds to actin filaments in vitro and
associates with stress fibers in cells. The VASP-actin interaction is
salt-sensitive, arguing for electrostatic interactions. Hence,
phosphorylation may significantly alter the actin binding properties of
VASP. This hypothesis was investigated by analyzing complex formation
of recombinant murine VASP with actin after phosphorylation with
cAMP-dependent kinase in different assays.
cAMP-dependent kinase phosphorylation had a negative effect
on both actin nucleation and VASP interaction with actin filaments,
with the actin nucleating capacity being more affected than actin
filament binding and bundling. Replacing VASP residues known to be
phosphorylated in vivo by acidic residues to mimic
phosphorylation had similar although less dramatic effects on
VASP-actin interactions. In contrast, phosphorylation had no significant effect on VASP oligomerization or its interaction with its
known ligands profilin, vinculin, and zyxin. When overexpressing VASP
mutants in eukaryotic cells, they all showed targeting to focal
contacts and stress fibers. Our results imply that VASP phosphorylation
may act as an immediate negative regulator of actin dynamics.
Phosphorylation of the Vasodilator-stimulated
Phosphoprotein Regulates Its Interaction with Actin*
*
This work was supported by the German Research Council.The costs of publication of this
article were defrayed in part by the payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Cell Biology,
Zoological Inst., Technical University of Braunschweig, Biocenter, Spielmannstr. 7, D-38092 Braunschweig, Germany. E-mail:
S.Illenberger@tu-bs.de.
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