Vasodilator-stimulated phosphoprotein

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VASP
Protein VASP PDB 1egx.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesVASP, vasodilator-stimulated phosphoprotein, vasodilator stimulated phosphoprotein
External IDsOMIM: 601703 MGI: 109268 HomoloGene: 7592 GeneCards: VASP
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for VASP
Genomic location for VASP
Band19q13.32Start45,506,579 bp[1]
End45,526,983 bp[1]
RNA expression pattern
PBB GE VASP 202205 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 7: 19.26 – 19.27 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

Function[edit]

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[edit]

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

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125753 - Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: VASP vasodilator-stimulated phosphoprotein".
  7. ^ a b c 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[edit]