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Cell Adh Migr. 2013 Nov-Dec;7(6):482-6. doi: 10.4161/cam.27351. Epub 2013 Dec 5.

Regulation of VASP by phosphorylation: consequences for cell migration.

Author information

1
Department of Cancer Biology; Mayo Clinic Comprehensive Cancer Center; Mayo Clinic; Jacksonville, FL USA.

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.

KEYWORDS:

VASP; cytoskeleton; filopodium; leading edge; migration; phosphorylation

PMID:
24401601
PMCID:
PMC3916352
DOI:
10.4161/cam.27351
[Indexed for MEDLINE]
Free PMC Article

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