Regulation of VASP by phosphorylation Consequences for cell migration

Heike Döppler, Peter Storz

Research output: Contribution to journalReview articlepeer-review

26 Scopus citations


Phosphorylations control all aspects of vasodilator-stimulated phosphoprotein (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.

Original languageEnglish (US)
Pages (from-to)482-486
Number of pages5
JournalCell Adhesion and Migration
Issue number6
StatePublished - Nov 2013


  • Cytoskeleton
  • Filopodium
  • Leading edge
  • Migration
  • Phosphorylation
  • VASP

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology


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