Actin filament tethering and bundling are important mechanisms involved in actin superstructure assembly. The ENA/VASP family includes VASP, mena, and Ena-Vasp-like (EVL). These multidomain proteins localize to the leading edge of filopodia where they associate with AFs, interact with profilin, and compete with capping proteins at the barbed end of AFs. Artificial relocalization of VASP from the plasma membrane to mitochondrial membranes inhibits filopodial formation and axon branching, while deletion of all three ENA/VASP proteins produces defects in cortical axon-tract formation. Regulation of VASP protein activity occurs through phosphorylation at Ser-157, Ser-239, and Thr-278. AMPK phosphorylates Thr-278, leading to impaired actin stress fiber assembly and changes in cell morphology.
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*For more information, see UniProt Accession P50552
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Stone, JD et al. (2016) J Non Invasive Vasc Invest. 1:2-9. (FC: rat ATr5 smooth muscle cells)
Tojkander, S. et al. (2015) Elife. Dec. 10, 4:e06126. (WB: human osteosarcoma)
Ke, Y. et al. (2015) Cell Microbiol. 17(4):473 (WB, IF: HEK293T)
Hocking, K. et al. (2013) PLoS ONE 8(4): e60986. (WB: porcine smooth muscle)
Kim, H.R. et al. (2010) AJP Cell Phys. 298:559. (WB: ferret dVSMCs)
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