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Upon T cell receptor engagement, the Src family kinases Lck and Fyn are recruited to the TCR complex via the CD3zeta chain, and inactivate phospholipase c-gamma. Phospholipase c-gamma is an enzyme that hydrolyzes phosphatidylinositol-4,5-bisphosphate (PIP2) and generates inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). IP3 and DAG are intracellular second messengers that activate a number of proteins, including the calcium-binding protein calmodulin and protein kinase C (PKC). IP3 is also known as a regulator of intracellular calcium ion concentrations. IP3 can open calcium channels in the plasma membrane, allowing the ions to enter into the cell. This change in intracellular calcium ion concentration can trigger activation of a number of downstream effectors and ultimately results in the cellular response of T cell activation (Liu et al. 2014). PKC is an important signaling molecule for the T cell. It is activated by the Ca2+-dependent phospholipase C and associates with the plasma membrane via its pleckstrin homology (PH) domain. The activated PKC is associated with both cytoskeletal and nuclear proteins through its C1 and C2 domains. PKC is activated upon TCR engagement and induces phosphorylation of a variety of substrates that are involved in T cell activation. Inhibition of PKC has been shown to cause inhibition of T cell activation.
The CD3 and CD3 chains are associated with the Lck and Fyn kinases and are essential for T cell activation, although the role of each component of the TCR complex is not yet well understood (Beeton et al. 2005). It has been postulated that the TCR complex can function as a molecular switch, regulating the downstream signaling pathways. For instance, the CD3 zeta chain has been shown to inhibit phospholipase c, and thus, inactivation of the TCR complex can reduce the activity of downstream signaling pathways (Beeton et al. 2005).
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