| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| As has been demonstrated with ActA , iActA also spontaneously inserted into the surface of mitochondria and induced recruitment of actin , alpha actinin , and the vasodilator stimulated phosphoprotein ( VASP ) to these subcellular organelles . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin based motility , the percentage of moving bacteria , and the localization of vasodilator stimulated phosphoprotein and profilin . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Listeria ActA surface protein contains a series of nearly identical EFPPPPTDE type oligoproline sequences for binding vasodilator stimulated phosphoprotein ( VASP ) . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Intracellular actin based motility of Listeria monocytogenes requires protein protein interactions involving two different proline rich sequences : first , the tightly bound bacterial surface protein ActA uses its multiple oligoproline registers [ consensus sequence = FE ( D ) FPPPPTD ( E ) E ( D ) ] to tether vasodilator stimulated phosphoprotein ( VASP ) to the bacterial surface ; and second , VASP then deploys its own multiple GPPPPP ( or GP 5 ) registers to localize the actin regulatory protein profilin to promote actin polymerization . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The actin based motilities of L . monocytogenes and S . flexneri are known to require the bacterial proteins ActA and IcsA , respectively , and several mammalian cytoskeleton proteins including the Arp2 / 3 complex and VASP ( vasodilator stimulated phosphoprotein ) for L . monocytogenes and vinculin and N WASP ( the neural Wiskott Aldrich syndrome protein ) for S . flexneri . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| A polyproline motif ( E / DFPPPPTD / E in the single letter amino acid code ) , present in the ActA protein of the intracellular bacterial pathogen Listeria monocytogenes , serves as a ligand for the Ena / VASP protein family the vasodilator stimulated phosphoprotein ( VASP ) , the murine protein Mena , Drosophila Enabled ( Ena ) and the Ena / VASP like protein Evl [ 4 ] [ 5 ] [ 6 ] [ 7 ] . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Here , we provide genetic and biochemical evidence that vasodilator stimulated phosphoprotein ( VASP ) recruitment by ActA can bypass defects in actin monomer binding . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| WASP WA and Scar WA ( which incorporate the actin and Arp2 / 3 binding regions of WASP and Scar 1 ) , to compete with endogenous WASP family members ; ( 2 ) . proline rich motifs ( PRM ) from the ActA protein of L . monocytogenes or from vinculin , which bind vasodilator stimulated phosphoprotein ( VASP ) , a regulator of cytoskeleton assembly . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The function of vasodilator stimulated phosphoprotein ( VASP ) in motility is analyzed using a biomimetic motility assay in which ActA coated microspheres propel themselves in a medium containing actin , the Arp2 / 3 complex , and three regulatory proteins in the absence or presence of VASP . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Only VASP is known to bind directly to ActA . ^^^ We sought to determine which regions of the ActA molecule interact with VASP and other components of the host microfilament system . ^^^ An ActA derivative from which the central proline rich repeats were deleted retained its ability to recruit filamentous actin , albeit poorly , but was unable to bind VASP . ^^^ 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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Purified VASP binds directly to the ActA polypeptide in vitro . ^^^ A ligand overlay blot using purified radiolabelled VASP enabled us to identify the ActA homologue of the related intracellular motile pathogen , Listeria ivanovii , as a protein with a molecular mass of approximately 150 kDa . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Recent evidence suggests the ActA analogue may act by displacing the profilin binding protein VASP ( Pistor , S . ^^^ Thus , the two structurally divergent bacteria , Listeria and Shigella , have adopted convergent mechanisms involving profilin recognition of VASP oligoproline sequences and VASP recognition of oligoproline sequences in ActA or an ActA like host protein to induce host cell actin assembly and to provide the force for intracellular locomotion and cell cell spread . . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The proline rich hinge domain could be exchanged for the analogous region of the ActA protein , and the number of such proline clusters , containing an FPPPP motif , correlated with the extent of VASP recruitment . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| A novel proline rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH 1 domain , a protein module present in the Ena / VASP family . ^^^ Two profilin binding proteins , VASP and Mena , are the only cellular proteins known so far to bind directly to ActA . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| VASP interacts with the central domain of ActA . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The EVH 1 ( Ena / VASP homology 1 ) domain of VASP is in slow association dissociation equilibrium high affinity binding to the zyxin homologous , proline rich region of ActA . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Determination of the VASP EVH 1 domain solution structure , together with peptide library screening , measurement of individual K ( d ) s by fluorescence titration , and NMR chemical shift mapping , revealed a second affinity determining epitope present in all four ActA EVH 1 binding motifs . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The only host cell protein known that directly interacts with ActA is the phosphoprotein VASP , which binds to the central proline rich repeat region of ActA . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| VASP is required for efficient propulsion of ActA coated beads in the reconstituted motility medium , but it does not affect the rates of barbed end branching / debranching by ActA activated Arp2 / 3 nor the capping of filaments . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The ActA protein is known to interact with several mammalian proteins including the phosphoprotein VASP , actin and the Arp2 / 3 complex . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| The VASP EVH 1 domain specifically binds peptides with the consensus motif FPPPP present in all its binding partners , including the Listerial ActA protein . ^^^ We have incorporated peptoid building blocks ( sarcosine derived , non natural amino acids ) into the peptide SFEFPPPPTEDEL from the Listerial ActA protein and were able to substitute the most highly conserved residues of this motif while maintaining binding to the VASP EVH 1 domain with affinities in the range of 45 180 microm . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we qualitatively examine the different actin gels produced when ActA fragments interact with either VASP or the Arp2 / 3 complex . . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| 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 . ^^^ |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P50552 and P68133 |
Pubmed |
SVM Score :0.0 |
| NA |
|