Vasodilator-stimulated phosphoprotein

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VASP
Protein VASP PDB 1egx.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases VASP
External IDs MGI: 109268 HomoloGene: 7592 GeneCards: VASP
RNA expression pattern
PBB GE VASP 202205 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001008736
NM_003370

NM_001282021
NM_001282022
NM_009499

RefSeq (protein)

NP_003361

Location (UCSC) Chr 19: 45.51 – 45.53 Mb Chr 7: 19.26 – 19.27 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Vasodilator-stimulated phosphoprotein is a protein that in humans is encoded by the VASP gene.[3][4]

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.[4]

Interactions[edit]

Vasodilator-stimulated phosphoprotein has been shown to interact with Zyxin,[5][6] Profilin 1[5] and PFN2.[5][7]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. 
  4. ^ a b "Entrez Gene: VASP vasodilator-stimulated phosphoprotein". 
  5. ^ 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. UNITED STATES. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740. 
  6. ^ 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. 
  7. ^ 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 398250Freely accessible. PMID 7737110. 

Further reading[edit]