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
Gene location (Human)
Chr.	Chromosome 19 (human)
End	45,526,983 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	19,005,742 bp
RNA expression pattern
	Top expressed in
	monocyte; ; saphenous vein; ; spleen; ; blood; ; rectum; ; thoracic aorta; ; ascending aorta; ; left uterine tube; ; right coronary artery; ; upper lobe of left lung;
	Top expressed in
	colon; ; spleen; ; left colon; ; left lung lobe; ; pyloric antrum; ; epithelium of stomach; ; atrium; ; duodenum; ; yolk sac; ; blood;
	More reference expression data
	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
	7408
	22323
	ENSG00000125753
	ENSMUSG00000030403
	P50552
	P70460
	NM_001008736 ; NM_003370
	NM_001282021 ; NM_001282022 ; NM_009499
	NP_003361
	NP_001268950 ; NP_001268951 ; NP_033525
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 16, 2023

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]

Related Research Articles

ENA/VASP homology proteins or EVH proteins are a family of closely related proteins involved in cell motility in vertebrate and invertebrate animals. EVH proteins are modular proteins that are involved in actin polymerization, as well as interactions with other proteins. Within the cell, Ena/VASP proteins are found at the leading edge of Lamellipodia and at the tips of filopodia. Ena, the founding member of the family was discovered in a drosophila genetic screen for mutations that act as dominant suppressors of the abl non receptor tyrosine kinase. Invertebrate animals have one Ena homologue, whereas mammals have three, named Mena, VASP, and Evl.

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.

Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the PIK3R1 gene.

Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.

Profilin-1 is a protein that in humans is encoded by the PFN1 gene.

Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

Ribosomal protein S6 kinase alpha-2 is an enzyme that in humans is encoded by the RPS6KA2 gene.

Zyxin is a protein that in humans is encoded by the ZYX gene.

Proto-oncogene tyrosine-protein kinase FER is an enzyme that in humans is encoded by the FER gene.

Protein enabled homolog is a protein that in humans is encoded by the ENAH gene.

FYN binding protein (FYB-120/130), also known as FYB, ADAP, and SLAP-130 is a protein that is encoded by the FYB gene in humans. The protein is expressed in T cells, monocytes, mast cells, macrophages, NK cells, but not B cells. FYB is a multifunctional protein involved in post-activation T cell signaling, lymphocyte cytokine production, cell adhesion, and actin remodeling.

Profilin-2 is a protein that in humans is encoded by the PFN2 gene.

Ena/VASP-like protein is a member of the Ena/VASP family of proteins that in humans is encoded by the EVL gene.

For the SSH-1 protocol, see Secure Shell#Version 1

Vinexin is a protein that in humans is encoded by the SORBS3 gene.

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.

Alpha-parvin is a protein that in humans is encoded by the PARVA gene.

Filamin-binding LIM protein 1 is a protein that in humans is encoded by the FBLIM1 gene.

<span class="mw-page-title-main">Actin assembly-inducing protein</span>

The Actin assembly-inducing protein (ActA) is a protein encoded and used by Listeria monocytogenes to propel itself through a mammalian host cell. ActA is a bacterial surface protein comprising a membrane-spanning region. In a mammalian cell the bacterial ActA interacts with the Arp2/3 complex and actin monomers to induce actin polymerization on the bacterial surface generating an actin comet tail. The gene encoding ActA is named actA or prtB.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125753 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030403 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
1 2 3 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.
↑ 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.
↑ 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.

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000125753 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid8812448-5] 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.

[entrez-6] 1 2 "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".

[pmid10882740-7] 1 2 3 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.

[pmid10801818-8] 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.

[pmid7737110-9] 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.

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Vasodilator-stimulated phosphoprotein

Contents

Function

Interactions

Related Research Articles

References

Further reading