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Stimulation of the T cell antigen receptor (TcR) results in protein tyrosine phosphorylation via non-receptor tyrosine kinases. The src-related p59[fyn] kinase is one such enzyme that associates with the TcR. Ligation of the TcR activates the protein kinase activity of p59[fyn] invarious human T cells. Fyn interacts with the CD3-ζ chains through its N-terminal region. In turn, fyn binds other proteins through its SH2 and SH3 domains. These proteins (p82 and p116) may serve as substrates and/or mediators of fyn activity. A 72kDa fyn-related protein binds to the TcR/CD3 complex in certain T cells. This protein, known as p72[fyn-R], is a variant of the fyn kinase and contains at least four novel Ser/Thr phosphorylation sites. These sites may make p72[fyn-R] less susceptible to the action of phosphatases than p59[fyn]. Like p59[fyn], p72[fyn-R] is constitutively associated with its receptor. The exact relationship between these two proteins is not yet clear. However, p72[fyn-R] immunoprecipitates with various antisera raised to either the N- or C-terminus of fyn. Similar to src and yes, fyn is highly expressed in brain. The localization of fyn in mouse brain and its interaction with myelin-associated glycoprotein (MAG) suggests that the fyn kinase has a role in the sensory network and in myelination during early stages of CNS formation.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
