Vasodilator-stimulated phosphoprotein is a
protein that in humans is encoded by the VASPgene.[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-terminalEVH2 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]
^"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.
PMID8812448.
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.
PMID1319722.
Vasodilator-stimulated phosphoprotein is a
protein that in humans is encoded by the VASPgene.[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-terminalEVH2 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]
^"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.
PMID8812448.
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.
PMID1319722.