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• W1558009066 abstract "We here identify protein kinase D (PKD) as an upstream regulator of the F-actin-binding protein cortactin and the Arp actin polymerization machinery. PKD phosphorylates cortactin in vitro and in vivo at serine 298 thereby generating a 14-3-3 binding motif. In vitro, a phosphorylation-deficient cortactin-S298A protein accelerated VCA-Arp-cortactin-mediated synergistic actin polymerization and showed reduced F-actin binding, indicative of enhanced turnover of nucleation complexes. In vivo, cortactin co-localized with the nucleation promoting factor WAVE2, essential for lamellipodia extension, in the actin polymerization zone in Heregulin-treated MCF-7 cells. Using a 3-dye FRET-based approach we further demonstrate that WAVE2-Arp and cortactin prominently interact at these structures. Accordingly, cortactin-S298A significantly enhanced lamellipodia extension and directed cell migration. Our data thus unravel a previously unrecognized mechanism by which PKD controls cancer cell motility." @default.
• W1558009066 created "2016-06-24" @default.
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• W1558009066 date "2010-06-01" @default.
• W1558009066 modified "2023-10-17" @default.
• W1558009066 title "Protein Kinase D Controls Actin Polymerization and Cell Motility through Phosphorylation of Cortactin" @default.
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• W1558009066 doi "https://doi.org/10.1074/jbc.m109.093880" @default.
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