| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.95514348 |
| In resting T cells , Csk is constitutively localized in lipid rafts by virtue of interaction with a phosphorylated adaptor protein , Csk binding protein ( Cbp ) / phosphoprotein associated with glycolipid enriched microdomains , and sets an activation threshold in TCR signaling . 0.95514348^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.61072973 |
| To establish the mechanism of Csk / Cbp mediated regulation of SFK in vivo , we observed dynamic changes in the interaction of Csk with Cbp by utilizing fusion proteins with modified green fluorescent proteins : cyan fluorescent protein ( CFP ) or yellow fluorescent protein ( YFP ) . 0.61072973^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.8686658 |
| Previous studies utilizing in vitro and transgenic models suggested that the Csk binding protein ( Cbp ) , also known as phosphoprotein associated with glycosphingolipid microdomains ( PAG ) , is the membrane adaptor for Csk . 0.8686658^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Here we present Cbp a transmembrane phosphoprotein that is ubiquitously expressed and binds specifically to the SH 2 domain of Csk . ^^^ Cbp is involved in the membrane localization of Csk and in the Csk mediated inhibition of c Src . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl terminal Src kinase , Csk . ^^^ Recently , we identified a transmembrane protein , Cbp ( Csk binding protein ) , that , when phosphorylated , can recruit Csk to the membrane where the SFKs are located . ^^^ The Cbp mediated relocation of Csk to the membrane may play a role in turning off the signaling events initiated by SFKs . ^^^ To further characterize the Csk Cbp interaction , we have generated a reconstituted system using soluble , highly purified proteins . ^^^ Csk and phosphorylated Cbp were co purified as a large protein complex consisting of at least four Csk . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| In resting peripheral T cells , Csk is constitutively present in lipid rafts through an interaction with the Csk SH 2 binding protein , PAG , also known as Cbp . ^^^ Upon triggering of the T cell antigen receptor ( TCR ) , PAG / Cbp is rapidly dephosphorylated leading to dissociation of Csk from lipid rafts . ^^^ However , tyrosine phosphorylation of PAG / Cbp resumes after 3 5 min , at which time Csk reassociates with the rafts . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Phosphoprotein associated with GEMs ( PAG ) , also known as Csk binding protein ( Cbp ) , is a broadly expressed palmitoylated transmembrane adapter protein found in membrane rafts , also called GEMs ( glycosphingolipid enriched membrane microdomains ) . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Transmembrane adapter proteins ( TRAPs ) are a relatively new and growing family of proteins that include linker for activation of T cells ( LAT ) , phosphoprotein associated with glycosphingolipid enriched micro domains ( PAG ) / C terminal Src kinase ( Csk ) binding protein ( Cbp ) , SHP 2 interacting transmembrane adapter protein ( SIT ) , T cell receptor interacting molecule ( TRIM ) , and the recently identified non T cell activation linker ( NTAL ) and pp 30 . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Cbp , a C terminal Src kinase ( Csk ) binding protein , is a transmembrane phosphoprotein that has been implicated in the regulation of the Src family kinase ( SFK ) through recruiting Csk , a negative regulator of SFK , to a membrane microdomain of lipid rafts . ^^^ The results obtained by using mutant mice or cells that lack Csk and / or a member of SFK , Fyn , reveal that Cbp is phosphorylated predominantly by raft localized Fyn in vivo . ^^^ Upon cell adhesion onto fibronectin , Cbp becomes transiently phosphorylated ( consistent with SFK activation ) and recruits Csk to lipid rafts . ^^^ In Csk deficient cells , continuous hyperactivation of SFK leads to continuous hyperphosphorylation of Cbp , accompanied by impaired cell spreading and migration . ^^^ These findings suggest that Cbp could serve as a sensor of SFK activity in early stages of cell adhesion signaling , and that Csk mediated down regulation of SFK is essential to allow dynamic cellular events involved in the regulation of cell spreading and migration . . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| In this study , we show that a recently identified transmembrane protein , Csk binding protein ( Cbp ) , also known as phospoprotein associated with glycosphingolipid enriched microdomains ( PAG ) , negatively regulates FcepsilonRI signaling . ^^^ In rat basophilic leukemia ( RBL ) 2H3 cells , the levels of tyrosine phosphorylation of Cbp / PAG and its association with Csk , a negative regulator for Lyn , significantly elevate immediately after aggregation of FcepsilonRI . ^^^ These findings combined with the fact that Cbp / PAG , Lyn , and aggregated FcepsilonRI are localized to lipid rafts , suggest that upon FcepsilonRI aggregation Cbp / PAG down regulates the receptor associated Lyn activity through relocating Csk to rafts , thereby efficiently mediating feedback inhibition of FcepsilonRI signaling . . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Src family PTKs are known to be present in glycolipid enriched microdomains ( GEMs ) , also called lipid rafts , and to be negatively regulated by PTK Csk complexed to tyrosine phosphorylated transmembrane adapter protein PAG ( phosphoprotein associated with GEMs ) also called Cbp ( Csk binding protein ) . ^^^ Proliferation arrest led to a striking increase of PAG / Cbp expression ; correspondingly , the amount of Csk associated with PAG / Cbp in GEMs increased markedly , whereas PTK Hck accumulation in GEM fractions did not alter on growth arrest . ^^^ We propose that Theileria induced lymphocyte proliferation and permanent activation of Hck stems from down regulation of PAG / Cbp and the concomitant constitutive loss of the negative regulator Csk from the GEMs of transformed B cells . . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Most transmembrane proteins are excluded from these specialized areas of membranes , notable exceptions being several palmitoylated proteins such as the T cell coreceptors CD 4 and CD 8 , and several recently described transmembrane adaptor proteins , LAT , non T cell activation linker ( NTAL ) / linker for activation of B cells ( LAB ) , phosphoprotein associated with GEMs ( PAG ) / Csk binding protein ( Cbp ) and LIME . ^^^ LAT is indispensable for TCR signaling ( and participates also at signal transduction initiated by some other receptors ) , NTAL / LAB appears to play a LAT like role in signaling initiated by BCR and some Fc receptors ; PAG / Cbp cooperates with Csk , the cytoplasmic tyrosine kinase negatively regulating Src family kinases . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Transmembrane adaptor protein PAG , also known as Csk binding protein ( Cbp ) , which binds and activates the cytoplasmic tyrosine kinase Csk , the major negative regulator of Src family kinases , was found to be expressed in germinal centers of lymphoid follicles as well as in follicular , but not mantle cell lymphomas . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The Csk binding protein ( Cbp ) localizes Csk close to its substrates at the plasma membrane , and increases the specific activity of the kinase . ^^^ To investigate this long range catalytic effect , the phosphorylation of Src and the conformation of Csk were investigated in the presence of a high affinity phosphopeptide derived from Cbp . ^^^ The binding of a small Cbp derived peptide to the SH 2 domain of Csk modifies these motions , enhancing Src recognition . . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Cbp deficiency alters Csk localization in lipid rafts but does not affect T cell development . ^^^ The ubiquitously expressed transmembrane adaptor Csk binding protein ( Cbp ) recruits Csk to lipid rafts , where the latter exerts its negative regulatory effect on the Src family of protein tyrosine kinases . ^^^ In contrast to Csk gene inactivation , which leads to embryonic lethality and impaired T cell development , Cbp deficient mice were viable and exhibited normal T cell development but with an increased thymocyte population . ^^^ In the absence of Cbp , the amount of Csk that localizes to the lipid rafts was greatly reduced . ^^^ |
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| Interacting proteins: P41240 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Csk binding protein ( Cbp ) negatively regulates epidermal growth factor induced cell transformation by controlling Src activation . ^^^ The Csk binding protein ( Cbp ) is a ubiquitously expressed transmembrane protein . ^^^ Here , we report that EGF stimulation induced Cbp tyrosine phosphorylation followed by Cbp Csk association , in a SFK dependent manner . ^^^ |
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