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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Vasodilator-stimulated phosphoprotein''' is a [[protein]] that in humans is encoded by the ''VASP'' [[gene]].<ref name="pmid8812448">{{cite journal |vauthors=Zimmer M, Fink T, Fischer L, Hauser W, Scherer K, Lichter P, Walter U | title = Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization | journal = Genomics | volume = 36 | issue = 2 | pages = 227–33 |date=January 1997 | pmid = 8812448 | pmc =  | doi = 10.1006/geno.1996.0457 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: VASP vasodilator-stimulated phosphoprotein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7408| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_VASP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1egx.
| PDB =
| Name = Vasodilator-stimulated phosphoprotein
| HGNCid = 12652
| Symbol = VASP
| AltSymbols =;
| OMIM = 601703
| ECnumber =
| Homologene = 7592
| MGIid = 109268
| GeneAtlas_image1 = PBB_GE_VASP_202205_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}}
| Component = {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7408
| Hs_Ensembl = ENSG00000125753
| Hs_RefseqProtein = NP_001008736
| Hs_RefseqmRNA = NM_001008736
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 50702528
| Hs_GenLoc_end = 50722076
| Hs_Uniprot = P50552
| Mm_EntrezGene = 22323
| Mm_Ensembl = ENSMUSG00000030403
| Mm_RefseqmRNA = NM_009499
| Mm_RefseqProtein = NP_033525
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 18416239
| Mm_GenLoc_end = 18423349
| Mm_Uniprot = P70460
}}
}}
{{SI}}
{{EH}}


==Overview==
Vasodilator-stimulated phosphoprotein (VASP) is a member of the [[Ena/Vasp homology proteins|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 domain|SH3]] and [[WW domain]]-containing proteins. Their [[C-terminus|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 [[cell motility|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 [[Protein kinase A|PKA]] and [[cGMP-dependent protein kinase|PKG]].<ref name="entrez" />
'''Vasodilator-stimulated phosphoprotein''', also known as '''VASP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VASP vasodilator-stimulated phosphoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7408| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
Vasodilator-stimulated phosphoprotein has been shown to [[Protein-protein interaction|interact]] with [[Zyxin]],<ref name=pmid10882740>{{cite journal |last=Harbeck |first=B |authorlink= |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10882740 |doi = 10.1074/jbc.M005066200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10801818>{{cite journal |last=Drees |first=B |authorlink= |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 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10801818 |doi = 10.1074/jbc.M001698200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Profilin 1]]<ref name=pmid10882740/>, and [[PFN2]].<ref name=pmid10882740/><ref name=pmid7737110>{{cite journal |last=Reinhard |first=M |authorlink= |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 |publisher= |location = ENGLAND| issn = 0261-4189| pmid = 7737110 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=398250 }}</ref>
| section_title =
| summary_text = 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]].<ref name="entrez">{{cite web | title = Entrez Gene: VASP vasodilator-stimulated phosphoprotein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7408| accessdate = }}</ref>
}}
==VASP-P==


The [[phosphorylation]] (P) of vasodilator-stimulated phosphoprotein (VASP) is a test based on flow cytometry which is very specific to the P2Y<sub>12</sub> signaling pathway. It is commercially available as a kit marketed as PLT VASP/P2Y<sub>12</sub> (BioCytex, Marseilles, France).
==References==
{{Reflist}}


VASP is an intracellular platelet protein that is not phosphorilated at baseline. VASP-P is mediated by the cAMP cascade, which is enhanced by [[prostaglandin]] E1 (PGE<sub>1</sub>) and inhibited by the link between ADP and P2Y<sub>12</sub> receptors. Therefore, VASP-P is a marker of P2Y<sub>12 </sub>receptor inhibition, whereas its non-phosphorylated counterpart correlates with the non-inhibited form of the P2Y<sub>12</sub> receptor.
==Further reading==
 
{{refbegin | 2}}
By using the PLT VASP/P2Y<sub>12</sub> kit, the effect of clopidogrel can be demonstrated by the persistence of VASP in its phosphorylated state (VASP-P) induced by PGE<sub>1</sub> despite the simultaneous addition of ADP.
*{{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=  | pmc=556672  }}
*{{cite journal  |vauthors=Halbrügge M, Eigenthaler M, Polke C, Walter U |title=Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes |journal=Cell. Signal. |volume=4 |issue= 2 |pages= 189–99 |year= 1992 |pmid= 1319722 |doi=10.1016/0898-6568(92)90082-J  }}
*{{cite journal  |vauthors=Reinhard M, Jouvenal K, Tripier D, Walter U |title=Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein) |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7956–60 |year= 1995 |pmid= 7644520 |doi=10.1073/pnas.92.17.7956  | pmc=41265  |bibcode=1995PNAS...92.7956R }}
*{{cite journal  |vauthors=Reinhard M, Giehl K, Abel K, etal |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 |year= 1995 |pmid= 7737110 |doi=  | pmc=398250  }}
*{{cite journal  |vauthors=Haffner C, Jarchau T, Reinhard M, etal |title=Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP |journal=EMBO J. |volume=14 |issue= 1 |pages= 19–27 |year= 1995 |pmid= 7828592 |doi=  | pmc=398048  }}
*{{cite journal  |vauthors=Horstrup K, Jablonka B, Hönig-Liedl P, etal |title=Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition |journal=Eur. J. Biochem. |volume=225 |issue= 1 |pages= 21–7 |year= 1994 |pmid= 7925440 |doi=10.1111/j.1432-1033.1994.00021.x  }}
*{{cite journal  |vauthors=Butt E, Abel K, Krieger M, etal |title=cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14509–17 |year= 1994 |pmid= 8182057 |doi=  }}
*{{cite journal  |vauthors=Laurent V, Loisel TP, Harbeck B, etal |title=Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes |journal=J. Cell Biol. |volume=144 |issue= 6 |pages= 1245–58 |year= 1999 |pmid= 10087267 |doi=10.1083/jcb.144.6.1245  | pmc=2150578  }}
*{{cite journal  |vauthors=Bachmann C, Fischer L, Walter U, Reinhard M |title=The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23549–57 |year= 1999 |pmid= 10438535 |doi=10.1074/jbc.274.33.23549  }}
*{{cite journal  |vauthors=Petit MM, Fradelizi J, Golsteyn RM, etal |title=LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity |journal=Mol. Biol. Cell |volume=11 |issue= 1 |pages= 117–29 |year= 2000 |pmid= 10637295 |doi=  10.1091/mbc.11.1.117| pmc=14761  }}
*{{cite journal  |vauthors=Krause M, Sechi AS, Konradt M, etal |title=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 |journal=J. Cell Biol. |volume=149 |issue= 1 |pages= 181–94 |year= 2000 |pmid= 10747096 |doi=10.1083/jcb.149.1.181  | pmc=2175102  }}
*{{cite journal  |vauthors=Drees B, Friederich E, Fradelizi J, etal |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 |year= 2000 |pmid= 10801818 |doi= 10.1074/jbc.M001698200 }}
*{{cite journal  |vauthors=Smolenski A, Poller W, Walter U, Lohmann SM |title=Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25723–32 |year= 2000 |pmid= 10851246 |doi= 10.1074/jbc.M909632199 }}
*{{cite journal  |vauthors=Harbeck B, Hüttelmaier S, Schluter K, etal |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30817–25 |year= 2000 |pmid= 10882740 |doi= 10.1074/jbc.M005066200 }}
*{{cite journal  |vauthors=Burkhardt M, Glazova M, Gambaryan S, etal |title=KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33536–41 |year= 2000 |pmid= 10922374 |doi= 10.1074/jbc.M005670200 }}
*{{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}}
*{{cite journal  |vauthors=Castellano F, Le Clainche C, Patin D, etal |title=A WASp-VASP complex regulates actin polymerization at the plasma membrane |journal=EMBO J. |volume=20 |issue= 20 |pages= 5603–14 |year= 2001 |pmid= 11598004 |doi= 10.1093/emboj/20.20.5603  | pmc=125672 }}
{{refend}}


More in detail, the [[blood]] sample is first incubated with PGE<sub>1</sub> alone or PGE<sub>1</sub> + ADP. Subsequently, after a cellular permeabilization, VASP-P is labeled by indirect no wash [[immunofluorescence]] using a specific monoclonal antibody. The two tested conditions are then evaluated by means of dual color [[flow cytometry]] analysis. Final results are usually expressed in terms of platelet reactivity index (PRI), which is calculated using corrected mean fluorescence intensities (MFIc) in the presence of PGE<sub>1</sub> alone or PGE<sub>1</sub> and ADP simultaneously, according to the following formula:
{{PDB Gallery|geneid=7408}}


PRI = [(MFIc<sub>PGE1</sub> - MFIc <sub>PGE1+ADP</sub>)/ MFIc<sub>PGE1</sub>]x100
[[Category:EVH1 domain]]


Assessment of VASP-P requires a low sample volume and is performed on whole [[blood]]. Another advantage is the opportunity to ship blood samples at room temperature to a central core laboratory. Ultimately, it correlates well with light transmittance aggregometry and [[VerifyNow]] technologies. However, sample preparation is time consuming and the reliability of the results is highly dependent from the presence of a skilled technician. Also, a flow cytometer is required.


==References==
{{Gene-19-stub}}
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
 
*{{cite journal  | author=Reinhard M, Halbrügge M, Scheer U, ''et al.'' |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=  }}
*{{cite journal  | author=Halbrügge M, Eigenthaler M, Polke C, Walter U |title=Protein phosphorylation regulated by cyclic nucleotide-dependent protein kinases in cell extracts and in intact human lymphocytes. |journal=Cell. Signal. |volume=4 |issue= 2 |pages= 189-99 |year= 1992 |pmid= 1319722 |doi=  }}
*{{cite journal  | author=Reinhard M, Jouvenal K, Tripier D, Walter U |title=Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7956-60 |year= 1995 |pmid= 7644520 |doi=  }}
*{{cite journal  | author=Reinhard M, Giehl K, Abel K, ''et al.'' |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 |year= 1995 |pmid= 7737110 |doi=  }}
*{{cite journal  | author=Haffner C, Jarchau T, Reinhard M, ''et al.'' |title=Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP. |journal=EMBO J. |volume=14 |issue= 1 |pages= 19-27 |year= 1995 |pmid= 7828592 |doi=  }}
*{{cite journal  | author=Horstrup K, Jablonka B, Hönig-Liedl P, ''et al.'' |title=Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition. |journal=Eur. J. Biochem. |volume=225 |issue= 1 |pages= 21-7 |year= 1994 |pmid= 7925440 |doi=  }}
*{{cite journal  | author=Butt E, Abel K, Krieger M, ''et al.'' |title=cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets. |journal=J. Biol. Chem. |volume=269 |issue= 20 |pages= 14509-17 |year= 1994 |pmid= 8182057 |doi=  }}
*{{cite journal  | author=Zimmer M, Fink T, Fischer L, ''et al.'' |title=Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization. |journal=Genomics |volume=36 |issue= 2 |pages= 227-33 |year= 1997 |pmid= 8812448 |doi= 10.1006/geno.1996.0457 }}
*{{cite journal  | author=Laurent V, Loisel TP, Harbeck B, ''et al.'' |title=Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. |journal=J. Cell Biol. |volume=144 |issue= 6 |pages= 1245-58 |year= 1999 |pmid= 10087267 |doi=  }}
*{{cite journal  | author=Bachmann C, Fischer L, Walter U, Reinhard M |title=The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23549-57 |year= 1999 |pmid= 10438535 |doi=  }}
*{{cite journal  | author=Petit MM, Fradelizi J, Golsteyn RM, ''et al.'' |title=LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. |journal=Mol. Biol. Cell |volume=11 |issue= 1 |pages= 117-29 |year= 2000 |pmid= 10637295 |doi=  }}
*{{cite journal  | author=Krause M, Sechi AS, Konradt M, ''et al.'' |title=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. |journal=J. Cell Biol. |volume=149 |issue= 1 |pages= 181-94 |year= 2000 |pmid= 10747096 |doi=  }}
*{{cite journal  | author=Drees B, Friederich E, Fradelizi J, ''et al.'' |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 |year= 2000 |pmid= 10801818 |doi= 10.1074/jbc.M001698200 }}
*{{cite journal  | author=Smolenski A, Poller W, Walter U, Lohmann SM |title=Regulation of human endothelial cell focal adhesion sites and migration by cGMP-dependent protein kinase I. |journal=J. Biol. Chem. |volume=275 |issue= 33 |pages= 25723-32 |year= 2000 |pmid= 10851246 |doi= 10.1074/jbc.M909632199 }}
*{{cite journal  | author=Harbeck B, Hüttelmaier S, Schluter K, ''et al.'' |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30817-25 |year= 2000 |pmid= 10882740 |doi= 10.1074/jbc.M005066200 }}
*{{cite journal  | author=Burkhardt M, Glazova M, Gambaryan S, ''et al.'' |title=KT5823 inhibits cGMP-dependent protein kinase activity in vitro but not in intact human platelets and rat mesangial cells. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33536-41 |year= 2000 |pmid= 10922374 |doi= 10.1074/jbc.M005670200 }}
*{{cite journal  | author=Ball LJ, Kühne R, Hoffmann B, ''et al.'' |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 }}
*{{cite journal  | author=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 }}
*{{cite journal  | author=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=  }}
*{{cite journal  | author=Castellano F, Le Clainche C, Patin D, ''et al.'' |title=A WASp-VASP complex regulates actin polymerization at the plasma membrane. |journal=EMBO J. |volume=20 |issue= 20 |pages= 5603-14 |year= 2001 |pmid= 11598004 |doi= 10.1093/emboj/20.20.5603 }}
}}
{{refend}}
{{SIB}}
{{WH}}
{{WikiDoc Sources}}

Latest revision as of 00:05, 27 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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View/Edit Human

Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.[1][2]

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.[2]

Interactions

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

References

  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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