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Gene Review

Vasp  -  vasodilator-stimulated phosphoprotein

Mus musculus

Synonyms: VASP, Vasodilator-stimulated phosphoprotein
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Disease relevance of Vasp


High impact information on Vasp

  • In Ena/VASP deficient cells, CP depletion resulted in ruffling instead of filopodia [4].
  • We propose a model for selection of lamellipodial versus filopodial organization in which CP is a negative regulator of filopodia formation and Ena/VASP has recruiting/activating functions downstream of actin filament elongation in addition to its previously suggested anticapping and antibranching activities [4].
  • In keratinocytes either null for alpha-catenin or blocked in VASP/Mena function, filopodia embed, but actin reorganization/polymerization is prevented, and membranes cannot seal [5].
  • Zyxin-null fibroblasts also show deficits in actin stress fiber remodeling and exhibit changes in the molecular composition of focal adhesions, most notably by severely reduced accumulation of Ena/VASP proteins [6].
  • The defects observed in the double knockout may also involve the family of Ena/Vasp proteins, which participate in actin cytoskeleton remodeling and interact with the WW domains of FE65 proteins [7].

Biological context of Vasp

  • Moreover, VASP-deficient cells show compromised migration and reorientation in a wound healing assay [8].
  • VASP(-/-) cells cover about twice the substrate surface area as wild type cells, while cell volumes are unchanged [8].
  • Analysis of invertebrate mutants implicates Ena/VASP function in several actin-dependent processes such as axon and dendritic guidance, cell migration, and dorsal closure [9].
  • Mice deficient in either Mena or VASP exhibit subtle defects in forebrain commissure formation and platelet aggregation, respectively [9].
  • These data show for the first time in vivo that VASP is involved in down-regulation of platelet adhesion to the vascular wall under both physiologic and pathophysiologic conditions [10].

Anatomical context of Vasp

  • Ena/vasodilator-stimulated phosphoprotein (VASP) proteins regulate the geometry of the actin cytoskeleton, thereby influencing cell morphology and motility [9].
  • Under physiologic conditions, platelet adhesion to endothelial cells was significantly enhanced in VASP null mutants when compared with wild-type mice (P <.05) [10].
  • Under pathophysiologic conditions, the loss of VASP increased platelet adhesion to the postischemic intestinal microvasculature, to the atherosclerotic endothelium of ApoE-deficient mice, and to the subendothelial matrix following endothelial denudation (P <.05 vs wild type) [10].
  • The results demonstrate that Ena-VASP proteins may play an important role in intercalated disk function at the interface between cardiac myocytes [2].
  • VASP is phosphorylated by both the cAMP- and cGMP-dependent protein kinases in a variety of cells, including platelets and smooth muscle cells [11].

Associations of Vasp with chemical compounds


Other interactions of Vasp


Analytical, diagnostic and therapeutic context of Vasp


  1. Accumulation of profilin II at the surface of Listeria is concomitant with the onset of motility and correlates with bacterial speed. Geese, M., Schlüter, K., Rothkegel, M., Jockusch, B.M., Wehland, J., Sechi, A.S. J. Cell. Sci. (2000) [Pubmed]
  2. Disruption of cardiac Ena-VASP protein localization in intercalated disks causes dilated cardiomyopathy. Eigenthaler, M., Engelhardt, S., Schinke, B., Kobsar, A., Schmitteckert, E., Gambaryan, S., Engelhardt, C.M., Krenn, V., Eliava, M., Jarchau, T., Lohse, M.J., Walter, U., Hein, L. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  3. Vasodilator-stimulated phosphoprotein-deficient mice demonstrate increased platelet activation but improved renal endothelial preservation and regeneration in passive nephrotoxic nephritis. Hohenstein, B., Kasperek, L., Kobelt, D.J., Daniel, C., Gambaryan, S., Renné, T., Walter, U., Amann, K.U., Hugo, C.P. J. Am. Soc. Nephrol. (2005) [Pubmed]
  4. Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Mejillano, M.R., Kojima, S., Applewhite, D.A., Gertler, F.B., Svitkina, T.M., Borisy, G.G. Cell (2004) [Pubmed]
  5. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Vasioukhin, V., Bauer, C., Yin, M., Fuchs, E. Cell (2000) [Pubmed]
  6. Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling. Hoffman, L.M., Jensen, C.C., Kloeker, S., Wang, C.L., Yoshigi, M., Beckerle, M.C. J. Cell Biol. (2006) [Pubmed]
  7. Essential roles for the FE65 amyloid precursor protein-interacting proteins in brain development. Guénette, S., Chang, Y., Hiesberger, T., Richardson, J.A., Eckman, C.B., Eckman, E.A., Hammer, R.E., Herz, J. EMBO J. (2006) [Pubmed]
  8. Increased spreading, Rac/p21-activated kinase (PAK) activity, and compromised cell motility in cells deficient in vasodilator-stimulated phosphoprotein (VASP). García Arguinzonis, M.I., Galler, A.B., Walter, U., Reinhard, M., Simm, A. J. Biol. Chem. (2002) [Pubmed]
  9. Mena and vasodilator-stimulated phosphoprotein are required for multiple actin-dependent processes that shape the vertebrate nervous system. Menzies, A.S., Aszodi, A., Williams, S.E., Pfeifer, A., Wehman, A.M., Goh, K.L., Mason, C.A., Fassler, R., Gertler, F.B. J. Neurosci. (2004) [Pubmed]
  10. Enhanced in vivo platelet adhesion in vasodilator-stimulated phosphoprotein (VASP)-deficient mice. Massberg, S., Grüner, S., Konrad, I., Garcia Arguinzonis, M.I., Eigenthaler, M., Hemler, K., Kersting, J., Schulz, C., Muller, I., Besta, F., Nieswandt, B., Heinzmann, U., Walter, U., Gawaz, M. Blood (2004) [Pubmed]
  11. The vasodilator-stimulated phosphoprotein (VASP) is involved in cGMP- and cAMP-mediated inhibition of agonist-induced platelet aggregation, but is dispensable for smooth muscle function. Aszódi, A., Pfeifer, A., Ahmad, M., Glauner, M., Zhou, X.H., Ny, L., Andersson, K.E., Kehrel, B., Offermanns, S., Fässler, R. EMBO J. (1999) [Pubmed]
  12. Aromatic and basic residues within the EVH1 domain of VASP specify its interaction with proline-rich ligands. Carl, U.D., Pollmann, M., Orr, E., Gertlere, F.B., Chakraborty, T., Wehland, J. Curr. Biol. (1999) [Pubmed]
  13. Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration. Loureiro, J.J., Rubinson, D.A., Bear, J.E., Baltus, G.A., Kwiatkowski, A.V., Gertler, F.B. Mol. Biol. Cell (2002) [Pubmed]
  14. Tissue-specific Spred-2 promoter activity characterized by a gene trap approach. Bundschu, K., Gattenlöhner, S., Knobeloch, K.P., Walter, U., Schuh, K. Gene Expr. Patterns (2006) [Pubmed]
  15. Functional characterization of green fluorescent protein-profilin fusion proteins. Wittenmayer, N., Rothkegel, M., Jockusch, B.M., Schlüter, K. Eur. J. Biochem. (2000) [Pubmed]
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