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A more recent version of this article appeared on August 1, 2003
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Submitted on January 27, 2003
Revised on March 21, 2003
Accepted on March 21, 2003
1 Institut für Allgemeine Zoologie und Genetik, Westfälische Wilhelms-Universität Münster, Schlossplatz 5, D-48149 Münster, Germany (present address: Institute of Biotechnology, Viikki Biocenter, FIN-00014 University of Helsinki, Finland)
2 Institut für Allgemeine Zoologie und Genetik, Westfälische Wilhelms-Universität Münster, Schlossplatz 5, D-48149 Münster, Germany
3 Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg, Austria
* Corresponding author. E-mail address: baehler{at}nwz.uni-muenster.de.
Functionally different subsets of actin filament arrays contribute to cellular organization and motility. We report the identification of a novel subset of loose actin filament arrays through regulated association with the widely expressed protein SWAP-70. These loose actin filament arrays were commonly located behind protruding lamellipodia and membrane ruffles. Visualization of these loose actin filament arrays was dependent on lamellipodial protrusion and the binding of the SWAP-70 PH-domain to a 3'-phosphoinositide. SWAP-70 with a functional PH-domain lacking the C-terminal 60 residues was targeted to the area of the loose actin filament arrays, but did not associate with actin filaments. The C-terminal 60 residues were sufficient for actin filament association, but provided no specificity for the subset of loose actin filament arrays. These results identify SWAP-70 as a PI 3-kinase signaling dependent marker for a distinct, hitherto unrecognised, array of actin filaments. Overexpression of SWAP-70 altered the actin organization and lamellipodial morphology. These alterations were dependent on a proper subcellular targeting of SWAP-70. We propose that SWAP-70 regulates the actin cytoskeleton as an effector or adaptor protein in response to agonist stimulated PI(3,4)P2 production and cell protrusion.
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