title: Regulation of VASP by phosphorylation: consequences for cell migration.
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.
authors.affiliation: Department of Cancer Biology; Mayo Clinic Comprehensive Cancer Center; Mayo Clinic; Jacksonville, FL USA.
authors.forename: Heike
authors.initials: H
authors.lastname: Döppler
authors.affiliation: Department of Cancer Biology; Mayo Clinic Comprehensive Cancer Center; Mayo Clinic; Jacksonville, FL USA.
authors.forename: Peter
authors.initials: P
authors.lastname: Storz
mesh_terms: D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002465:Cell Movement / Q000502:physiology*; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D015815:Cell Adhesion Molecules; D008840:Microfilament Proteins; D010750:Phosphoproteins; D011493:Protein Kinase C
keywords: VASP; cytoskeleton; filopodium; leading edge; migration; phosphorylation