Vasodilator-stimulated phosphoprotein

Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an N-terminal EVH1 domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions cell membranes. In the mid-region of the protein, family members have a proline-rich region that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.

Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin,{{cite journal |last=Harbeck |first=B |author2=Hüttelmaier S |author3=Schluter K |author4=Jockusch B M |author5=Illenberger S |date=October 2000 |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin |journal=J. Biol. Chem. |volume=275 |issue=40 |pages=30817–25 | issn = 0021-9258| pmid = 10882740 |doi = 10.1074/jbc.M005066200 |doi-access=free }}{{cite journal |last=Drees |first=B |author2=Friederich E |author3=Fradelizi J |author4=Louvard D |author5=Beckerle M C |author6=Golsteyn R M |date=July 2000 |title=Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins |journal=J. Biol. Chem. |volume=275 |issue=29 |pages=22503–11 | issn = 0021-9258| pmid = 10801818 |doi = 10.1074/jbc.M001698200 |doi-access=free }} Profilin 1, and PFN2.{{cite journal |last=Reinhard |first=M |author2=Giehl K |author3=Abel K |author4=Haffner C |author5=Jarchau T |author6=Hoppe V |author7=Jockusch B M |author8=Walter U |date=April 1995 |title=The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins |journal=EMBO J. |volume=14 |issue=8 |pages=1583–9 | issn = 0261-4189| pmid = 7737110 |pmc=398250 |doi=10.1002/j.1460-2075.1995.tb07146.x }}

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• {{cite journal |vauthors=Reinhard M, Halbrügge M, Scheer U, etal |title=The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts |journal=EMBO J. |volume=11 |issue= 6 |pages= 2063–70 |year= 1992 |pmid= 1318192 |doi= 10.1002/j.1460-2075.1992.tb05264.x| pmc=556672 }}
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• {{cite journal |vauthors=Ball LJ, Kühne R, Hoffmann B, etal |title=Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity |journal=EMBO J. |volume=19 |issue= 18 |pages= 4903–14 |year= 2000 |pmid= 10990454 |doi= 10.1093/emboj/19.18.4903 | pmc=314220 }}
• {{cite journal |vauthors=Bearer EL, Prakash JM, Manchester RD, Allen PG |title=VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations |journal=Cell Motil. Cytoskeleton |volume=47 |issue= 4 |pages= 351–64 |year= 2001 |pmid= 11093254 |doi= 10.1002/1097-0169(200012)47:4<351::AID-CM8>3.0.CO;2-8 |pmc=3376085}}
• {{cite journal |vauthors=Lawrence DW, Pryzwansky KB |title=The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading |journal=J. Immunol. |volume=166 |issue= 9 |pages= 5550–6 |year= 2001 |pmid= 11313394 |doi= 10.4049/jimmunol.166.9.5550|doi-access=free }}
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Category:EVH1 domain

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