Vasodilator-stimulated phosphoprotein

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Identifiers
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External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
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Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.[1][2]

## Contents

* 1 Function
* 2 Interactions
* 3 References
* 4 Further reading

## Function

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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.[2]

## Interactions

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Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin,[3][4] Profilin 1[3], and PFN2.[3][5]

## References

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1. ↑ Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U (January 1997). "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization". Genomics. 36 (2): 227–33. doi:10.1006/geno.1996.0457. PMID 8812448.
2. ↑ 2.0 2.1 "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
3. ↑ 3.0 3.1 3.2 Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. UNITED STATES. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
4. ↑ Drees, B; Friederich E; Fradelizi J; Louvard D; Beckerle M C; Golsteyn R M (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. UNITED STATES. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. ISSN 0021-9258. PMID 10801818.
5. ↑ Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. ENGLAND. 14 (8): 1583–9. ISSN 0261-4189. PMC 398250. PMID 7737110.

## Further reading

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* Reinhard M, Halbrügge M, Scheer U, et al. (1992). "The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts". EMBO J. 11 (6): 2063–70. PMC 556672. PMID 1318192.
* Halbrügge M, Eigenthaler M, Polke C, Walter U (1992). "Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes". Cell. Signal. 4 (2): 189–99. doi:10.1016/0898-6568(92)90082-J. PMID 1319722.
* Reinhard M, Jouvenal K, Tripier D, Walter U (1995). "Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7956–60. Bibcode:1995PNAS...92.7956R. doi:10.1073/pnas.92.17.7956. PMC 41265. PMID 7644520.
* Reinhard M, Giehl K, Abel K, et al. (1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. PMC 398250. PMID 7737110.
* Haffner C, Jarchau T, Reinhard M, et al. (1995). "Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP". EMBO J. 14 (1): 19–27. PMC 398048. PMID 7828592.
* Horstrup K, Jablonka B, Hönig-Liedl P, et al. (1994). "Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition". Eur. J. Biochem. 225 (1): 21–7. doi:10.1111/j.1432-1033.1994.00021.x. PMID 7925440.
* Butt E, Abel K, Krieger M, et al. (1994). "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets". J. Biol. Chem. 269 (20): 14509–17. PMID 8182057.
* Laurent V, Loisel TP, Harbeck B, et al. (1999). "Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes". J. Cell Biol. 144 (6): 1245–58. doi:10.1083/jcb.144.6.1245. PMC 2150578. PMID 10087267.
* Bachmann C, Fischer L, Walter U, Reinhard M (1999). "The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation". J. Biol. Chem. 274 (33): 23549–57. doi:10.1074/jbc.274.33.23549. PMID 10438535.
* Petit MM, Fradelizi J, Golsteyn RM, et al. (2000). "LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity". Mol. Biol. Cell. 11 (1): 117–29. doi:10.1091/mbc.11.1.117. PMC 14761. PMID 10637295.
* Krause M, Sechi AS, Konradt M, et al. (2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton". J. Cell Biol. 149 (1): 181–94. doi:10.1083/jcb.149.1.181. PMC 2175102. PMID 10747096.
* Drees B, Friederich E, Fradelizi J, et al. (2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
* Smolenski A, Poller W, Walter U, Lohmann SM (2000). "Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I". J. Biol. Chem. 275 (33): 25723–32. doi:10.1074/jbc.M909632199. PMID 10851246.
* Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
* Burkhardt M, Glazova M, Gambaryan S, et al. (2000). "KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells". J. Biol. Chem. 275 (43): 33536–41. doi:10.1074/jbc.M005670200. PMID 10922374.
* Ball LJ, Kühne R, Hoffmann B, et al. (2000). "Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity". EMBO J. 19 (18): 4903–14. doi:10.1093/emboj/19.18.4903. PMC 314220. PMID 10990454.
* Bearer EL, Prakash JM, Manchester RD, Allen PG (2001). "VASP protects actin filaments from gelsolin: an in vitro study with implications for platelet actin reorganizations". Cell Motil. Cytoskeleton. 47 (4): 351–64. doi:10.1002/1097-0169(200012)47:4<351::AID-CM8>3.0.CO;2-8. PMC 3376085. PMID 11093254.
* Lawrence DW, Pryzwansky KB (2001). "The vasodilator-stimulated phosphoprotein is regulated by cyclic GMP-dependent protein kinase during neutrophil spreading". J. Immunol. 166 (9): 5550–6. doi:10.4049/jimmunol.166.9.5550. PMID 11313394.
* Castellano F, Le Clainche C, Patin D, et al. (2001). "A WASp-VASP complex regulates actin polymerization at the plasma membrane". EMBO J. 20 (20): 5603–14. doi:10.1093/emboj/20.20.5603. PMC 125672. PMID 11598004.

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PDB gallery

* 1egx: SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

1egx: SOLUTION STRUCTURE OF THE ENA-VASP HOMOLOGY 1 (EVH1) DOMAIN OF HUMAN VASODILATOR-STIMULATED PHOSPHOPROTEIN (VASP)

* 1usd: HUMAN VASP TETRAMERISATION DOMAIN L352M

1usd: HUMAN VASP TETRAMERISATION DOMAIN L352M

* 1use: HUMAN VASP TETRAMERISATION DOMAIN

1use: HUMAN VASP TETRAMERISATION DOMAIN

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