Protein kinase C (PKC)-θ is a serine/threonine kinase belonging to the calcium-independent novel PKC subfamily; its expression is restricted to certain tissues and cell types, including T cells. The signals delivered from T cell receptor (TCR) and CD28 costimulatory molecules trigger PKC-θ catalytic activation and membrane translocation to the immune logical synapse, leading to activation of NF-κB, AP-1, and NF-AT.These transcription factors are important forT cell survival, activation, and differentiation. Phosphorylation of PKC-θ at multiple Ser/Thr/Tyr residues is induced inT cells duringTCR signaling. Some phosphorylation sites play critical roles in the regulation of PKC-θ function and downstream signaling. The regulation mechanisms for PKC-θ phosphorylation sites are now being revealed. In this review, we discuss the current understanding of the regulation of PKC-θ function by phosphorylation duringTCR signaling.
Date:
2012-07
Relation:
Frontiers in Immunology. 2012 Jul;3:Article number 197.
