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• W2055281063 abstract "Phosphorylations control all aspects of vasodilator-stimulated phospho-protein (VASP) function. Mapped phosphorylation sites include Y39, S157, S239, T278, and S322, and multiple kinases have been shown to mediate their phosphorylation. Recently, Protein Kinase D1 (PKD1) as a direct kinase for S157 and S322 joined this group. While S157 phosphorylation generally seems to serve as a signal for membrane localization, phosphorylations at S322 or at S239 and T278 have opposite effects on F-actin accumulation. In migrating cells, S322 phosphorylation increases filopodia numbers and length, while S239/T278 phosphorylations decrease these and also disrupt formation of focal adhesions. Therefore, the kinases mediating these phosphorylations can be seen as switches needed to facilitate cell motility." @default.
• W2055281063 created "2016-06-24" @default.
• W2055281063 creator A5062388236 @default.
• W2055281063 creator A5064581175 @default.
• W2055281063 date "2013-11-19" @default.
• W2055281063 modified "2023-10-18" @default.
• W2055281063 title "Regulation of VASP by phosphorylation" @default.
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• W2055281063 doi "https://doi.org/10.4161/cam.27351" @default.
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