Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Under conditions of increased detergent stringency Sam 68 , Wiskott Aldrich Syndrome protein , and hnRNP K , but not Cbl and Fyn , were bound to the Itk SH 3 domain . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Interaction between Sam 68 and Src family tyrosine kinases , Fyn and Lck , in T cell receptor signaling . ^^^ Sam 68 was associated with the Src homology 2 and 3 domains of Fyn and also those of another Src family kinase , Lck . ^^^ These data suggest that Sam 68 participates in the signal transduction pathway downstream of TCR coupled Src family kinases Fyn and Lck in lymphocytes , that is not only in the mitotic pathway downstream of c Src in fibroblasts . . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
The mammalian members include Sam 68 , which is a target of Src , Fyn , and Grb 2 , and the newly cloned mouse quaking proteins ( qkI ) necessary in early embryogenesis and myelination . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
A direct interaction between Sam 68 and the two src kinases involved in T cell activation , p 59 ( fyn ) and p 56 ( lck ) , as well as a partnership of Sam 68 with various key downstream signaling molecules , like phospholipase Cgamma 1 and Grb 2 , has been shown . ^^^ We conclude that p 59 ( fyn ) and p 56 ( lck ) differently participate in regulating the phosphorylation state of Sam 68 in T cells and that ZAP 70 may contribute to Sam 68 tyrosine phosphorylation and to the specific recruitment of this molecule after CD 3 stimulation . . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
The interaction and colocalization of Sam 68 with the splicing associated factor YT 521 B in nuclear dots is regulated by the Src family kinase p 59 ( fyn ) . ^^^ The Src family kinase p 59 ( fyn ) mediated tyrosine phosphorylation of Sam 68 negatively regulates its association with YT 521 B , and overexpression of p 59 ( fyn ) dissolves nuclear dots containing YT 521 B . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Here we demonstrate that the proposed adapter protein for Src kinases , Sam 68 , is a ligand whose proline rich motifs interact with the SH 3 domains of p 59 ( fyn ) and phospholipase Cgamma 1 as well as with the WW domains of FBP 30 and FBP 21 . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Immunoprecipitation and in vitro kinase assays reveal rapid GC induced down modulation of Lck and Fyn kinases using SAM 68 ( Src [ pp60c src ] associated in mitosis 68 kDa ) as a substrate . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
NA |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Fyn membrane localization is necessary to induce the constitutive tyrosine phosphorylation of Sam 68 in the nucleus of T lymphocytes . ^^^ By overexpressing the two proteins , we show that the constitutive phosphorylation of Sam 68 in vivo directly correlates with cellular Fyn levels , but not with Lck expression , despite the capacity of the PTK to strongly phosphorylate the molecule in vitro . ^^^ We find that Sam 68 phosphorylation , including in the nuclear fraction in which the molecule is predominantly expressed , is lost with a delocalized Fyn mutant deleted of its N terminal membrane anchoring domain . ^^^ We conclude that the constitutive phosphorylation of Sam 68 in T cells is a Fyn dependent process occurring in a cell membrane compartment from which phospho Sam 68 molecules can thereafter accumulate into the nucleus . . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
The distinct capacity of Fyn and Lck to phosphorylate Sam 68 in T cells is essentially governed by SH3 / SH2 catalytic domain linker interactions . ^^^ Sam 68 phosphorylation correlates with Fyn but not Lck expression in T cells . ^^^ We show that this specificity is not based on a spatial segregation of the two kinases , since a chimeric Lck molecule containing the membrane anchoring domain of Fyn does not phosphorylate Sam 68 . ^^^ In T cells , Fyn appears to be the active Src kinase in rafts , but Sam 68 is not expressed in rafts , and its distinct phosphorylation by Fyn and Lck is not affected by raft dispersion . ^^^ Thus , the distinct potential of Fyn and Lck to phosphorylate Sam 68 is likely controlled by the interaction of the kinase SH 3 domain with the linker and Sam 68 , possibly on a competitive binding basis . . ^^^ |
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Interacting proteins: Q07666 and P06241 |
Pubmed |
SVM Score :0.0 |
Tr kit promotes the formation of a multimolecular complex composed by Fyn , PLCgamma 1 and Sam 68 . ^^^ Western blot analysis indicates that one of these proteins is Sam 68 , an RNA binding protein that is known to interact with and be phosphorylated by Src like kinases in mitosis . tr kit promotes the association of Sam 68 with PLCgamma 1 and Fyn in a multimolecular complex , as demonstrated by co immunoprecipitation of the phosphorylated forms of these proteins using antibodies directed to anyone of the partners of the complex . ^^^ Expression of tr kit potentiates the interaction of endogenous Sam 68 also with the SH 3 domain of Fyn . ^^^ Furthermore , the subcellular localization of Sam 68 is affected by tr kit through activation of Fyn in live cells . ^^^ Lastly , we show that interaction with the SH 3 domain of Fyn triggers the release of Sam 68 from bound RNA . ^^^ |
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