Vasodilator-stimulated phosphoprotein

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Vasodilator-stimulated phosphoprotein
Protein VASP PDB 1egx.png
PDB rendering based on 1egx.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbol VASP
External IDs OMIM601703 MGI109268 HomoloGene7592 GeneCards: VASP Gene
RNA expression pattern
PBB GE VASP 202205 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7408 22323
Ensembl ENSG00000125753 ENSMUSG00000030403
UniProt P50552 P70460
RefSeq (mRNA) NM_001008736 NM_009499
RefSeq (protein) NP_003361 NP_033525
Location (UCSC) Chr 19:
46.01 – 46.03 Mb
Chr 7:
19.26 – 19.27 Mb
PubMed search [1] [2]

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

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.[2]

Interactions[edit]

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

References[edit]

  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. ^ a b "Entrez Gene: VASP vasodilator-stimulated phosphoprotein". 
  3. ^ 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. 
  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[edit]