| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.93692862 |
| Immunoprecipitation experiments revealed that Cbl associates with Hck in Bac1 . 2F5 cells , while expression of an activated form of Hck in Bac1 . 2F5 cells induces tyrosine phosphorylation of Cbl in the absence of lipopolysaccharide stimulation . 0.93692862^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Cbl was observed to bind to bacterial fusion proteins encoding the unique , SH 3 , and SH 2 domains of Fyn , Hck , and Lyn . ^^^ This was not the case for the SH 2 domain of Hck , however , as binding of the Hck fusion protein to Cbl appeared to require multiple domains . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| In hck / fgr / lyn / triple mutant cells , which are defective in spreading on fibronectin coated surfaces in vitro and show impaired migration in vivo , Cbl tyrosine phosphorylation is blocked , Cbl protein levels are low , adhesion dependent translocation of Cbl to the membrane is impaired and Cbl associated , membrane localized phosphatidylinositol 3 ( PI 3 ) kinase activity is dramatically reduced . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Aggregation of FcgammaRIIa , the low affinity receptor for monomeric IgG , activates nonreceptor protein tyrosine kinases such as Lyn , Hck , and Syk , potentially driving the phosphorylation of the downstream adaptor proteins , including Cbl and / or Nck . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Binding studies indicated that Cbl could bind to glutathione S transferase ( GST ) fusion proteins encoding the unique , Src homology domain 3 ( SH 3 ) , and SH 2 domains of Fyn , Hck , or Lyn . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| The proto oncogene p 120 ( Cbl ) is a downstream substrate of the Hck protein tyrosine kinase . ^^^ We have found that upon enzymatic activation of Hck by the heavy metal mercuric chloride , there was a rapid increase in the levels of tyrosine phosphorylation of several proteins including the proto oncogene p 120 ( Cbl ) . ^^^ Fibroblasts that are transformed with an activated allele of Hck exhibit constitutive Cbl phosphorylation . ^^^ Hck phosphorylates Cbl in vitro and the interaction between Cbl and Hck is direct , requiring Hck ' s unique , SH 3 and SH 2 domains for optimal binding . ^^^ Using a novel estrogen regulated chimera of Hck we have shown a hormone dependent association between Hck and Cbl in murine fibroblasts . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Indeed , CD 38 ligation on monocytes induces tyrosine phosphorylation of several intracellular proteins including the protooncogene product c cbl and the fgr and hck tyrosine kinases . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Tyrosine phosphorylation of Vav and c Cbl was restored in common by a Lyn , a Hck , and a Src , but Fc gamma RIIB tyrosine phosphorylation , which is implicated in negative signaling , was reconstituted solely by a Lyn and a Hck . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Membrane anchored Cbl suppresses Hck protein tyrosine kinase mediated cellular transformation . ^^^ Herein we show that Cbl can negatively regulate another signaling molecule , namely theSrc family kinase Hck by targeting it for degradation . ^^^ Hck mediated cellular transformation of murine fibroblasts is reverted by ectopic expression of a membrane anchored allele of Cbl as assessed by the cellular morphology , suppression of anchorage independent growth , and an overall reduction in the total tyrosine phosphorylation levels within the cells . ^^^ The expression of Cbl at the plasma membrane targets both Hck and itself for ubiquitination and degradation , requiring an intact RING finger . ^^^ Activated Hck and membrane anchored Cbl are present in similar subcellular localizations and co immunoprecipitate , suggesting that their interaction is required for subsequent ubiquitination and degradation . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Cloning of the p95Cbl cDNA revealed that it contains a deletion resulting in the loss of 111 amino acids , eliminating two critical tyrosine residues in the linker region as well as the entire RING finger domain . p95Cbl displays a propensity for its interaction with the Src family kinase Hck over cellular Cbl expressed in the same cells . ^^^ |
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| Interacting proteins: P08631 and P22681 |
Pubmed |
SVM Score :0.0 |
| Instead , both PMA treated wild type and hck ( / ) fgr ( / ) macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both . ^^^ Moreover , c cbl ( / ) macrophages displayed the same impairment of motility as hck ( / ) fgr ( / ) macrophages and a similar morphology with less polarization and more dorsal ruffling than wild type macrophages . ^^^ As Hck and Fgr expression and activity were not decreased in c cbl ( / ) macrophages , these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase regulated macrophage motility pathway . . ^^^ |
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