Regulation of VASP by phosphorylation: consequences for cell migration

H Döppler, P Storz - Cell adhesion & migration, 2013 - Taylor & Francis
H Döppler, P Storz
Cell adhesion & migration, 2013Taylor & Francis
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 …
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.
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