| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.9387274 |
| VASP ( vasodilator stimulated phosphoprotein ) , a protein associated with microfilaments at cellular contact sites , has been identified as a ligand for profilin and zyxin , two proteins also involved in microfilament dynamics and organization at these regions . 0.9387274^^^ VASP ( vasodilator stimulated phosphoprotein ) , a protein associated with microfilaments at cellular contact sites , has been identified as a ligand for profilin and zyxin , two proteins also involved in microfilament dynamics and organization at these regions . 0.68127252^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.69646366 |
| By transfection assays we showed that zyxin interaction with Mena / VASP in vivo enhances the production of actin rich structures at the apical surface of cells . 0.69646366^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Identification , purification , and characterization of a zyxin related protein that binds the focal adhesion and microfilament protein VASP ( vasodilator stimulated phosphoprotein ) . ^^^ Together with our recent identification of VASP as a natural ligand of the profilin poly ( L proline ) binding site , our present results suggest that , by linking profilin to zyxin / p83 , VASP may participate in spatially confined profilin regulated F actin formation . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| VASP binds to the focal adhesion proteins vinculin and zyxin and this probably directs the phosphoprotein to focal adhesions and the leading edge of stimulated cells . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| A missense mutation that resulted in an amino acid substitution in the EVH 1 domain eliminated in vitro binding of Ena to the cytoskeletal protein zyxin , a previously reported binding partner of VASP . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Vinculin did not colocalize with VASP on motile virions and remained in focal adhesion contacts ; however , another ABM 1 containing host protein , zyxin , was concentrated at the rear of motile virions . ^^^ VASP and zyxin were redistributed dramatically several hours before the formation of actin rocket tails , concentrating in the viral factories of the perinuclear cytoplasm . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| To further investigate the underlying mechanism of actin tail assembly , we examined the localization of components of the actin cytoskeleton including Arp 3 , VASP , vinculin and zyxin during vaccinia , Listeria and Shigella infections . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Cdc 42 induced protrusions were enriched in the vasodilator stimulated phosphoprotein VASP and the focal adhesion associated proteins zyxin and ezrin . ^^^ Our data suggest that Cdc 42 induced actin based protrusions result from the local and serial recruitment of cytoskeletal proteins including zyxin , VASP , and ezrin . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| VASP , which is expressed in most cell types and in particularly high levels in human platelets , binds to profilin , zyxin , vinculin , F actin , and the Listeria monocytogenes surface protein ActA . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Opposing cell surfaces are clamped by desmosomes , while vinculin , zyxin , VASP , and Mena are recruited to adhesion zippers by a mechanism that requires alpha catenin . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Here we demonstrate that stimulation of human umbilical vein endothelial cells ( HUVECs ) by both ANP and 8 ( 4 chlorophenylthio ) guanosine 3 ' : 5 ' monophosphate ( 8 pCPT cGMP ) activates transfected cGK 1 and causes detachment of VASP and its known binding partner ( zyxin ) from focal adhesions in > 60 % of cells after 30 min . ^^^ These results indicate that cGK 1 phosphorylation of VASP results in loss of VASP and zyxin from focal adhesions , a response that could contribute to cGK alteration of cytoskeleton regulated processes such as cell migration . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| In contrast , phosphorylation had no significant effect on VASP oligomerization or its interaction with its known ligands profilin , vinculin , and zyxin . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| We propose that this epitope , which is absent in the sequences of the native EVH 1 interaction partners zyxin and vinculin , may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| We found that human zyxin and the related protein ActA of Listeria monocytogenes can generate new actin structures in a vasodilator stimulated phosphoprotein dependent ( VASP ) manner , but independently of the Arp2 / 3 complex . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Zyxin is not colocalized with vasodilator stimulated phosphoprotein ( VASP ) at lamellipodial tips and exhibits different dynamics to vinculin , paxillin , and VASP in focal adhesions . ^^^ One candidate recently implicated in these processes is the LIM domain protein zyxin , which can bind both Ena / vasodilator stimulated phosphoprotein ( VASP ) proteins and the actin filament cross linking protein alpha actinin . ^^^ Together , these data identify zyxin as an early target for signals leading to adhesion disassembly , but exclude its role in recruiting Ena / VASP proteins to the tips of lamellipodia and filopodia . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| We quantitatively determined the amounts of laminin , fibronectin , vitronectin , and thrombospondin secreted by these glioma cell lines in vitro , as well as the amount of each of the eight beta integrin subunits and the adhesion complex related molecules , including talin , vinculin , profilin , zyxin , alpha actinin , paxillin , and VASP . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ Furthermore , lanthanum / zinc treatment also facilitated the early onset of actin based vaccinia motility , a process that also utilizes Arp2 / 3 and N WASP for nucleation and the zyxin VASP profilin complex for efficient elongation . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Zyxin is an evolutionarily conserved protein that is concentrated at sites of cell adhesion , where it associates with members of the Enabled ( Ena ) / vasodilator stimulated phosphoprotein ( VASP ) family of cytoskeletal regulators and is postulated to play a role in cytoskeletal dynamics and signaling . ^^^ Because zyxin contributes to the localization of Ena / VASP family members at certain subcellular locations , we carefully examined the zyxin ( / ) mice for evidence of defects that have been observed when Ena / VASP proteins are compromised in the mouse . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Expression of VASP and zyxin in cochlear pillar cells : indication for actin based dynamics . ^^^ In these processes zyxin acts as an important partner of VASP and is particularly concentrated at sites where VASP dependent actin dynamics occur . ^^^ Based on indirect evidence that actin mediated dynamics may effect the mechanical properties of the cochlea , we have investigated expression of VASP and zyxin in the postnatal and adult rat cochlea using polymerase chain reaction and Western blot approaches , as well as immunohistochemistry and confocal microscopy . ^^^ Besides an expected expression in vessels and fibroblasts , VASP and zyxin expression was also observed in pillar cells . ^^^ In pillar cells , VASP and zyxin were co localised with pan actin , suggesting actin based dynamics in these cochlear cells , which until now were rather presumed to form a highly rigid bridge between the inner and outer sensory cells . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| The COOH terminal half recruits zyxin as well as Mena and VASP from cell extracts . ^^^ However , using RNAi ablation , we demonstrate that zyxin is required to recruit Tes , as well as Mena and VASP , but not vinculin or paxillin , to focal adhesions . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| By using green fluorescent protein ( GFP ) fusion constructs , the recruitment of the Arp2 / 3 complex , vasodilator stimulated phosphoprotein ( VASP ) , Neural Wiskott Aldrich syndrome protein ( N WASP ) , zyxin , vinculin , paxillin and alpha actinin to the surface of B . pseudomallei and into corresponding actin tails was studied . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Ena VASP proteins share an identical domain organization with an NH 2 terminal Ena VASP homology ( EVH 1 ) domain , which mediates the binding of these proteins to FPPPP motif containing partners such as zyxin and vinculin . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Overlay studies demonstrate that LASP 1 directly binds to the proline rich domains of zyxin , lipoma preferred partner ( LPP ) , and vasodilator stimulated phosphoprotein ( VASP ) , with zyxin being the most prominent interacting partner . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| TES interacts with a variety of cytoskeletal proteins including zyxin , mena , VASP , talin and actin . ^^^ We have also used RNAi to examine the requirement of TES and zyxin for each other ' s localisation at focal adhesions , and we propose a hierarchy of recruitment , with zyxin being first , followed by VASP and then TES . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Mechanical stress also induces the rapid zyxin dependent mobilization of vasodilator stimulated phosphoprotein from focal adhesions to actin filaments . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| Previous work implicated VASP in assembly of cell cell junctions in keratinocytes and the VASP binding protein zyxin colocalizes with VASP at cell cell junctions . ^^^ Using a quantitative assay for cell cell adhesion , we demonstrate that zyxin and LPP function to increase the rate of early cell cell junction assembly through the VASP binding ActA repeat region . ^^^ Dominant negative zyxin / LPP mutants reduce the rate of adhesion , lower VASP levels in detergent insoluble cadherin actin networks , and allow for the accumulation of capping protein at cell cell contacts . ^^^ These data implicate the LIM domains of zyxin and LPP in regulating cell cell junction assembly through VASP . . ^^^ |
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| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15942 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
|