PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28783324-0 2017 A Noncanonical Binding Site in the EVH1 Domain of Vasodilator-Stimulated Phosphoprotein Regulates Its Interactions with the Proline Rich Region of Zyxin. Proline 124-131 vasodilator stimulated phosphoprotein Homo sapiens 50-87 28783324-6 2017 Here, quantitative nuclear magnetic resonance titration analysis reveals a dominant bivalent 1:1 (Zyxin:EVH1) interaction between the Zyxin proline rich region and the VASP EVH1 domain that utilizes the EVH1 canonical binding site and a novel secondary binding site on the opposite face of the EVH1 domain. Proline 140-147 vasodilator stimulated phosphoprotein Homo sapiens 168-172 25848013-2 2015 Particularly abundant, yet so far undruggable, targets include domains specialized in recognizing proline-rich segments, including Src-homology 3 (SH3), WW, GYF, and Drosophila enabled (Ena)/vasodilator-stimulated phosphoprotein (VASP) homology 1 (EVH1) domains. Proline 98-105 vasodilator stimulated phosphoprotein Homo sapiens 230-234 18001770-9 2008 Peptide blotting using a series of designed peptides with profilins 1 and 2a indicates differences between the two profilins towards proline-rich peptides from mDia1 and VASP. Proline 133-140 vasodilator stimulated phosphoprotein Homo sapiens 170-174 25246528-11 2014 We also found that the interaction of profilin-actin complexes with the VASP-proline-rich domain and the binding of the VASP-F-actin binding domain to the side of growing filaments is critical for transforming actin polymerization into motion. Proline 77-84 vasodilator stimulated phosphoprotein Homo sapiens 72-76 23076992-3 2013 To accomplish these functions, zyxin recruits VASP to cellular sites via proline-rich binding sites near zyxin"s amino terminus. Proline 73-80 vasodilator stimulated phosphoprotein Homo sapiens 46-50 23076992-5 2013 Here we assess how zyxin-VASP binding through both the proline rich motifs and the LIM domains alters specific VASP functions. Proline 55-62 vasodilator stimulated phosphoprotein Homo sapiens 25-29 23076992-5 2013 Here we assess how zyxin-VASP binding through both the proline rich motifs and the LIM domains alters specific VASP functions. Proline 55-62 vasodilator stimulated phosphoprotein Homo sapiens 111-115 18413140-2 2008 VASP is recruited to sites of actin dynamics by interactions with proline rich FPPPPP motifs. Proline 66-73 vasodilator stimulated phosphoprotein Homo sapiens 0-4 12429845-8 2002 WASP- and Scar1-coated bead motility rates were significantly reduced by depletion of profilin and VASP and could be more efficiently rescued by a combination of VASP and wild-type profilin than by VASP and a mutant profilin that cannot bind proline-rich sequences. Proline 242-249 vasodilator stimulated phosphoprotein Homo sapiens 99-103 16987806-3 2006 VASP was initially characterized as a proline-rich substrate of protein kinases A and G in human platelets and later shown to be a scaffold protein, regulating both signal transduction pathways and the actin filament system. Proline 38-45 vasodilator stimulated phosphoprotein Homo sapiens 0-4 16531412-6 2006 The interaction is mediated by the VASP EVH1 domain and a single L104PPPPP site located within the migfilin proline-rich domain. Proline 108-115 vasodilator stimulated phosphoprotein Homo sapiens 35-39 14983521-5 2004 Using a synthetic peptide array, two discrete binding sites for VASP were identified within palladin"s proline-rich amino-terminal domain. Proline 103-110 vasodilator stimulated phosphoprotein Homo sapiens 64-68 12441356-5 2003 We found that the LIM domains are the main focal adhesion targeting elements and that the proline-rich region of LPP, which harbors binding sites for alpha-actinin and vasodilator-stimulated phosphoprotein (VASP), has a weak targeting capacity. Proline 90-97 vasodilator stimulated phosphoprotein Homo sapiens 168-205 12441356-5 2003 We found that the LIM domains are the main focal adhesion targeting elements and that the proline-rich region of LPP, which harbors binding sites for alpha-actinin and vasodilator-stimulated phosphoprotein (VASP), has a weak targeting capacity. Proline 90-97 vasodilator stimulated phosphoprotein Homo sapiens 207-211 12451594-6 2003 Efficient elongation was found to require zyxin, VASP, and profilin, proteins that interact by means of their ABM-1 and ABM-2 proline-rich motifs. Proline 126-133 vasodilator stimulated phosphoprotein Homo sapiens 49-53 12429845-8 2002 WASP- and Scar1-coated bead motility rates were significantly reduced by depletion of profilin and VASP and could be more efficiently rescued by a combination of VASP and wild-type profilin than by VASP and a mutant profilin that cannot bind proline-rich sequences. Proline 242-249 vasodilator stimulated phosphoprotein Homo sapiens 162-166 12429845-8 2002 WASP- and Scar1-coated bead motility rates were significantly reduced by depletion of profilin and VASP and could be more efficiently rescued by a combination of VASP and wild-type profilin than by VASP and a mutant profilin that cannot bind proline-rich sequences. Proline 242-249 vasodilator stimulated phosphoprotein Homo sapiens 162-166 12023040-1 2002 EVH1 (enabled VASP (vasodilator-stimulated protein) homology 1)/WH1 (WASP (Wiskott-Aldrich syndrome protein) homology 1) domains, present in Ena VASP and WASP, are protein interaction modules specialised in binding proline-rich ligands. Proline 215-222 vasodilator stimulated phosphoprotein Homo sapiens 14-18 12134077-4 2002 The proline-rich region, the putative G-actin binding site, and the Ser/Thr phosphorylation of Ena/VASP proteins are all required for efficient Listeria motility. Proline 4-11 vasodilator stimulated phosphoprotein Homo sapiens 99-103 12023040-1 2002 EVH1 (enabled VASP (vasodilator-stimulated protein) homology 1)/WH1 (WASP (Wiskott-Aldrich syndrome protein) homology 1) domains, present in Ena VASP and WASP, are protein interaction modules specialised in binding proline-rich ligands. Proline 215-222 vasodilator stimulated phosphoprotein Homo sapiens 20-50 12023040-1 2002 EVH1 (enabled VASP (vasodilator-stimulated protein) homology 1)/WH1 (WASP (Wiskott-Aldrich syndrome protein) homology 1) domains, present in Ena VASP and WASP, are protein interaction modules specialised in binding proline-rich ligands. Proline 215-222 vasodilator stimulated phosphoprotein Homo sapiens 145-149 8980130-0 1996 VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs. Proline 71-78 vasodilator stimulated phosphoprotein Homo sapiens 0-4 11598004-5 2001 An in vitro analysis demonstrates that the proline-rich domain of WASp binds VASP with an affinity of approximately 10(6) M(-1). Proline 43-50 vasodilator stimulated phosphoprotein Homo sapiens 77-81 11810195-1 2001 Vasodilator-stimulated phosphoprotein (VASP) and mammalian Enabled (Mena) are members of the proline-rich Ena/VASP protein family that links the cell membrane proteins, signal transduction pathways, and the actin cytoskeleton. Proline 93-100 vasodilator stimulated phosphoprotein Homo sapiens 0-37 11810195-1 2001 Vasodilator-stimulated phosphoprotein (VASP) and mammalian Enabled (Mena) are members of the proline-rich Ena/VASP protein family that links the cell membrane proteins, signal transduction pathways, and the actin cytoskeleton. Proline 93-100 vasodilator stimulated phosphoprotein Homo sapiens 39-43 11810195-1 2001 Vasodilator-stimulated phosphoprotein (VASP) and mammalian Enabled (Mena) are members of the proline-rich Ena/VASP protein family that links the cell membrane proteins, signal transduction pathways, and the actin cytoskeleton. Proline 93-100 vasodilator stimulated phosphoprotein Homo sapiens 110-114 10801818-2 2000 We screened the entire amino acid sequence of human zyxin for Mena-interacting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequences capable of binding to Ena/vasodilator-stimulated phosphoprotein (VASP) family members in vitro. Proline 118-125 vasodilator stimulated phosphoprotein Homo sapiens 193-234 10801818-6 2000 Microinjection into cells of peptides corresponding to the first proline-rich sequence of zyxin caused the loss of Mena/VASP from focal contacts. Proline 65-72 vasodilator stimulated phosphoprotein Homo sapiens 120-124 10801818-8 2000 We conclude that zyxin and proteins that harbor similar proline-rich repeats contribute to the positioning of Mena/VASP proteins. Proline 56-63 vasodilator stimulated phosphoprotein Homo sapiens 115-119 8980130-3 1996 Competition experiments with a vinculin-derived peptide showed that a proline-rich motif, located in the hinge region that connects vinculin"s head and tail domains, is involved in VASP binding. Proline 70-77 vasodilator stimulated phosphoprotein Homo sapiens 181-185 8836115-0 1996 The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Proline 77-84 vasodilator stimulated phosphoprotein Homo sapiens 19-56 8836115-0 1996 The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Proline 77-84 vasodilator stimulated phosphoprotein Homo sapiens 58-62 8836115-3 1996 The bacterial protein ActA binds VASP via a proline-rich motif that is very similar to a sequence in the proline-rich region of the focal-adhesion protein vinculin. Proline 44-51 vasodilator stimulated phosphoprotein Homo sapiens 33-37 8836115-3 1996 The bacterial protein ActA binds VASP via a proline-rich motif that is very similar to a sequence in the proline-rich region of the focal-adhesion protein vinculin. Proline 105-112 vasodilator stimulated phosphoprotein Homo sapiens 33-37 8836115-4 1996 We have examined the ability of VASP, synthesized using an in vitro transcription/translation system, to bind to a series of vinculin peptides expressed as glutathione S-transferase fusion proteins, and have shown that it binds specifically to the proline-rich region in vinculin. Proline 248-255 vasodilator stimulated phosphoprotein Homo sapiens 32-36 8836115-5 1996 Using immobilized peptides corresponding to the two proline-rich motifs within this domain, the VASP-binding site was localized to proline-rich motif-l (residues 839-850). Proline 52-59 vasodilator stimulated phosphoprotein Homo sapiens 96-100 8836115-5 1996 Using immobilized peptides corresponding to the two proline-rich motifs within this domain, the VASP-binding site was localized to proline-rich motif-l (residues 839-850). Proline 131-138 vasodilator stimulated phosphoprotein Homo sapiens 96-100 7583101-11 1995 The listerial ActA polypeptide contains at least two essential sites that are required for efficient microfilament assembly: an amino-terminal 23 amino-acid region for actin filament nucleation, and VASP-binding proline-rich repeats. Proline 212-219 vasodilator stimulated phosphoprotein Homo sapiens 199-203 7737110-0 1995 The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. Proline 4-11 vasodilator stimulated phosphoprotein Homo sapiens 58-62 7737110-3 1995 The recent molecular cloning of the vasodilator-stimulated phosphoprotein (VASP), an established in vivo substrate of cAMP- and cGMP-dependent protein kinases, revealed the presence of a proline-rich domain which prompted us to investigate a possible interaction with profilins. Proline 187-194 vasodilator stimulated phosphoprotein Homo sapiens 36-73 7737110-3 1995 The recent molecular cloning of the vasodilator-stimulated phosphoprotein (VASP), an established in vivo substrate of cAMP- and cGMP-dependent protein kinases, revealed the presence of a proline-rich domain which prompted us to investigate a possible interaction with profilins. Proline 187-194 vasodilator stimulated phosphoprotein Homo sapiens 75-79 7737110-5 1995 Here, we demonstrate that VASP is a natural proline-rich profilin ligand. Proline 44-51 vasodilator stimulated phosphoprotein Homo sapiens 26-30 7737110-7 1995 Moreover, VASP and a novel protein were specifically extracted from total cell lysates by profilin affinity chromatography and subsequently eluted either with poly-L-proline or a peptide corresponding to a proline-rich VASP motif. Proline 166-173 vasodilator stimulated phosphoprotein Homo sapiens 10-14 35076015-0 2022 Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH. Proline 7-14 vasodilator stimulated phosphoprotein Homo sapiens 83-87 35076015-4 2022 A pocket on the ENAH EVH1 domain that has diverged from other Ena/VASP paralogs recognizes extended SLiMs and favors motif-flanking proline residues. Proline 132-139 vasodilator stimulated phosphoprotein Homo sapiens 66-70