| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.50106706 |
| Immunofluorescence analysis demonstrated that activation of PKCalpha by phorbol 12 myristate 13 acetate ( PMA ) , or ectopic expression of constitutively activated PKCalpha , directs AFAP 110 to colocalize with and bind to the c Src SH 3 domain , resulting in activation of the tyrosine kinase . 0.50106706^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The actin filament associated protein AFAP 110 is an SH2 / SH3 binding partner for Src . ^^^ Thus , AFAP 110 may be positioned to modulate the effects of Src upon actin filaments . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Mechanical stretch increased tyrosine phosphorylation of rat AFAP and its binding to c Src within the initial several minutes . ^^^ On the basis of the molecular structure of AFAP protein , we speculate that it is an adaptor in mechanical stretch induced activation of c Src . ^^^ Src SH 2 and SH 3 binding motifs are highly conserved in the AFAP proteins ( from chicken , rat to human ) . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Recent reports indicate that the Src SH2 / SH3 binding partner AFAP 110 has the capacity to modulate actin filament integrity as a cSrc activating protein and as an actin filament bundling protein . ^^^ As the expression pattern of AFAP overlaps with the reported expression patterns of cSrc and Fyn , we hypothesize that AFAP is positioned to modulate signal transduction cascades that direct activation of these nonreceptor tyrosine kinases and concomitant cellular changes that occur in actin filaments during brain development . . ^^^ Protein expression levels of the Src activating protein AFAP are developmentally regulated in brain . ^^^ We sought to identify the localization of AFAP in mouse brain in order to identify its expression pattern and potential role as a cellular modulator of Src family kinase activity and actin filament integrity in the brain . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Here we show that mechanical stretch induced c Src protein tyrosine kinase activation is mediated through the actin filament associated protein ( AFAP ) . ^^^ Distributed along the actin filaments , AFAP can directly active c Src through binding to its Src homology 3 and / or 2 domains . ^^^ Mutations at these specific binding sites on AFAP blocked mechanical stretch induced c Src activation . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The actin filament associated protein ( AFAP 1 10 ) forms a stable complex with activated variants of the Pp60c src ( Src ) non receptor tyrosine kinase through SH 2 and SH 3 interactions . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| A variant form of the Src SH2 / SH3 binding partner AFAP 110 is detected in brain and contains a novel internal sequence which binds to a 67 kDa protein . ^^^ Recently , the cDNA sequence of a novel Src and Fyn binding protein called AFAP 110 , for Actin Filament Associated Protein 110 kDa , was reported . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The actin filament associated protein , AFAP 110 , is a Src SH2 / SH3 binding partner that can modulate changes in actin filament structure . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The Yes SH 3 domain was unable to affinity absorb the Src SH3 / SH2 binding partner AFAP 110 from COS 1 cell lysates , and chimeric constructs of Src527F containing the cYes SH 3 domain were unable to efficiently co immunoprecipitate with AFAP 110 from chicken embryo fibroblasts . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| In vitro analysis of AFAP 110 binding to bacterium encoded glutathione S transferase ( GST ) fusion proteins revealed that AFAP 110 present in normal cell extracts binds efficiently to Src SH3 / SH2 containing fusion proteins , less efficiently to Src SH 3 containing proteins , and poorly to SH 2 containing fusion proteins . ^^^ In contrast , AFAP 110 in Src transformed cell extracts bound to GST SH3 / SH2 and GST SH 2 fusion proteins . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The integrity of the SH 3 binding motif of AFAP 110 is required to facilitate tyrosine phosphorylation by , and stable complex formation with , Src . ^^^ The actin filament associated protein AFAP 110 forms a stable complex with activated variants of Src in chick embryo fibroblast cells . ^^^ These data indicate that both SH 2 and SH 3 domains may work cooperatively to facilitate Src / AFAP 110 stable complex formation . ^^^ As a test for this hypothesis , we sought to understand whether one or both SH 3 binding motifs in AFAP 110 modulate interactions with the Src SH 3 domain and if this interaction was required to present AFAP 110 for tyrosine phosphorylation by , and stable complex formation with , Src . ^^^ Co expression of activated Src ( pp 60 ( 527F ) ) with AFAP 110 in Cos 1 cells permit tyrosine phosphorylation of AFAP 110 and stable complex formation with pp 60 ( 527F ) . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Co expression of Src527F , unlike cSrc , will abrogate affinity absorption of AFAP 110 with GST cterm . ^^^ Deletion of only the leucine zipper region of the carboxy terminal alpha helix ( 44 amino acids ) from AFAP 110 ( AFAPAdeltazip ) demonstrate that both AFAPdeltalzip and actin filaments are repositioned into rosette like structures , similar to the effects of Src527F , while co expression of AFAP 110 with cSrc will not affect actin filaments . ^^^ Src can regulate carboxy terminal interactions with AFAP 110 , which influence self association , cell localization and actin filament integrity . ^^^ The SH 2 and SH 3 binding partner AFAP 110 is a tyrosine phosphorylated substrate of Src . ^^^ AFAP 110 has been hypothesized to link Src to actin filaments , which may contribute to the effects of Src upon actin filament integrity . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Recent data has indicated that AFAP 110 may also serve to activate cSrc in response to this conformational change as well . ^^^ The actin filament associated protein of 110 kDa ( AFAP 110 ) was first identified as an SH3 / SH2 binding partner for the nonreceptor tyrosine kinase , Src . ^^^ Subsequent data have demonstrated that AFAP 110 can interact with other Src family members . ^^^ Thus AFAP 110 may function as an adaptor protein by linking Src family members and / or other signaling proteins to actin filaments . ^^^ Thus , AFAP 110 may function in several ways by ( 1 ) acting as an adaptor protein that links signaling molecules to actin filaments , ( 2 ) serving as a platform for the construction of larger signaling complexes , ( 3 ) serving as an activator of Src family kinases in response to cellular signals that alter its conformation and ( 4 ) directly effecting actin filament organization as an actin filament cross linking protein . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| We hypothesize that cellular signals which alter AFAP 110 conformation , enable it to activate cellular kinases such as cSrc , which then direct changes in actin filament integrity in a Rho dependent fashion . . ^^^ The actin filament associated protein of 110 kDa ( AFAP 110 ) is a Src binding partner that represents a potential modulator of actin filament integrity in response to cellular signals . ^^^ Deletion of the leucine zipper motif of AFAP 110 ( AFAP 110 ( Deltalzip ) ) has been shown to induce a phenotype which resembles Src transformed cells , by repositioning actin filaments into rosettes . ^^^ This deletion also mimics a conformational change in AFAP 110 that is detected in Src transformed cells . ^^^ The results presented here indicate that unlike AFAP 110 , AFAP 110 ( Deltalzip ) is capable of activating cellular tyrosine kinases , including Src family members , and that AFAP 110 ( Deltalzip ) itself is hyperphosphorylated . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| The actin filament associated protein and Src binding partner , AFAP 110 , is an adaptor protein that links signaling molecules to actin filaments . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| Deletion of the Lzip motif ( AFAP 110 ( Deltalzip ) ) reduces the stability of the AFAP 110 multimer and concomitantly increases its ability to crosslink actin filaments , in vitro , and to activate cSrc and alter actin filament integrity , in vivo . ^^^ In vivo , only AFAP 110 ( Deltalzip ) and AFAP 110 ( 581P ) were to activate cSrc and to alter cellular actin filament integrity . ^^^ These data indicate that the intrinsic ability of AFAP 110 to crosslink actin filaments is dependent upon both the sequence and structure of the Lzip motif , while the ability of the Lzip motif to regulate AFAP 110 directed activation of cSrc and changes in actin filament integrity in vivo is dependent upon the structure or presence of the Lzip motif . ^^^ We hypothesize that the intrinsic ability of AFAP 110 to crosslink actin filaments or activate cSrc are distinct functions . . ^^^ |
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| Interacting proteins: Q8N556 and P12931 |
Pubmed |
SVM Score :0.0 |
| NA |
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