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• W2079399291 abstract "The Src family protein tyrosine kinase Fyn (p59fyn) plays an important role in thymocyte development and T cell receptor (TCR) signal transduction. Fyn has been shown to associate with the TCR-CD3 complex, the protein tyrosine phosphatase CD45 and several co-receptors such as CD28 which are crucial for initiating T cell activation and proliferation. The molecular basis of how Fyn is associated with these transmembrane proteins is largely unknown. To investigate the Fyn association with the TCR-CD3 complex, CD45 and CD28 at the molecular level, various Fyn/beta-galactosidase fusion proteins were constructed and expressed in Jurkat cells. Co-localization experiments applying antibody-induced co-capping and double immunofluorescence staining techniques were used to study the association of these fusion proteins with the TCR-CD3 complex, CD45 and CD28. Our results revealed that co-localization of Fyn with the TCR-CD3 complex requires the unique N terminus whereas co-localization with CD45 depends on the unique N terminus, the Src homology (SH)3- and a functional SH2 domain. CD28 co-localizes with Fyn molecules that contain the N terminus and a functional SH2 domain. These results suggest that Fyn association with the TCR-CD3 complex, CD45 and CD28 is mediated by different molecular mechanisms." @default.
• W2079399291 created "2016-06-24" @default.
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• W2079399291 creator A5047613604 @default.
• W2079399291 creator A5090559397 @default.
• W2079399291 date "1997-10-01" @default.
• W2079399291 modified "2023-10-16" @default.
• W2079399291 title "Co-localization of Fyn with CD3 complex, CD45 or CD28 depends on different mechanisms" @default.
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• W2079399291 doi "https://doi.org/10.1002/eji.1830271025" @default.
• W2079399291 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9368621" @default.
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