Vasodilator-stimulated phosphoprotein

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Vasodilator-stimulated phosphoprotein
PDB rendering based on 1egx.
Available structures: 1egx, 1usd, 1use
Identifiers
Symbol(s) VASP;
External IDs OMIM: 601703 MGI: 109268 HomoloGene: 7592
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 7408 22323
Ensembl ENSG00000125753 ENSMUSG00000030403
Uniprot P50552 P70460
Refseq NM_001008736 (mRNA)
NP_001008736 (protein)		 NM_009499 (mRNA)
NP_033525 (protein)
Location Chr 19: 50.7 - 50.72 Mb Chr 7: 18.42 - 18.42 Mb
Pubmed search [1] [2]

Vasodilator-stimulated phosphoprotein, also known as VASP, is a human gene.[1]

Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain 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.[1]

[edit] References

  1. ^ a b Entrez Gene: VASP vasodilator-stimulated phosphoprotein.

[edit] Further reading

  • 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. 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. 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. 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. 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. 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. 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. 
  • Zimmer M, Fink T, Fischer L, et al. (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. 
  • 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. 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. 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. 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. 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. 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. 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. 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. PMID 11598004. 
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