Vasodilator-stimulated phosphoprotein

VASP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1EGX, 1USD, 1USE, 2PAV, 2PBD, 3CHW
Identifiers
Aliases	VASP , vasodilator-stimulated phosphoprotein, vasodilator stimulated phosphoprotein
External IDs	OMIM: 601703; MGI: 109268; HomoloGene: 7592; GeneCards: VASP; OMA:VASP - orthologs
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19q13.32 Start 45,506,579 bp [1] End 45,526,983 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7|7 A3 Start 18,990,854 bp [2] End 19,005,742 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte monocyte mucosa of transverse colon saphenous vein spleen blood muscle layer of sigmoid colon rectum thoracic aorta ascending aorta Top expressed in granulocyte mesenteric lymph nodes tibiofemoral joint colon spleen left colon left lung lobe pyloric antrum epithelium of stomach atrium More reference expression data BioGPS More reference expression data
Gene ontology Molecular function profilin binding SH3 domain binding protein binding actin binding cadherin binding Cellular component cell projection membrane focal adhesion bicellular tight junction filopodium plasma membrane cell junction actin cytoskeleton extracellular exosome cytoskeleton lamellipodium membrane lamellipodium filopodium membrane cytoplasm cytosol Biological process positive regulation of actin filament polymerization axon guidance neural tube closure actin polymerization or depolymerization protein homotetramerization actin cytoskeleton organization cell junction assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7408 22323 Ensembl ENSG00000125753 ENSMUSG00000030403 UniProt P50552 P70460 RefSeq (mRNA) NM_001008736 NM_003370 NM_001282021 NM_001282022 NM_009499 RefSeq (protein) NP_003361 NP_001268950 NP_001268951 NP_033525 Location (UCSC) Chr 19: 45.51 – 45.53 Mb Chr 7: 18.99 – 19.01 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene. ^{[5] [6]}

Function

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. ^[6]

Interactions

Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin, ^{[7] [8]} Profilin 1, ^[7] and PFN2. ^{[7] [9]}

References

1. GRCh38: Ensembl release 89: ENSG00000125753 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030403 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
7. 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. 275 (40): 30817–25. doi: 10.1074/jbc.M005066200 . ISSN   0021-9258. PMID   10882740.
8. 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. 275 (29): 22503–11. doi: 10.1074/jbc.M001698200 . ISSN   0021-9258. PMID   10801818.
9. 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. 14 (8): 1583–9. doi:10.1002/j.1460-2075.1995.tb07146.x. ISSN   0261-4189. PMC   398250 . PMID   7737110.

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. doi:10.1002/j.1460-2075.1992.tb05264.x. 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. doi:10.1002/j.1460-2075.1995.tb07146.x. 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. doi:10.1002/j.1460-2075.1995.tb06971.x. 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. doi: 10.1016/S0021-9258(17)36652-8 . 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.