[HTML][HTML] Regulation of PKC-θ function by phosphorylation in T cell receptor signaling

X Wang, HC Chuang, TH Tan - Frontiers in immunology, 2012 - frontiersin.org
X Wang, HC Chuang, TH Tan
Frontiers in immunology, 2012frontiersin.org
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 immunological
synapse, leading to activation of NF-κB, AP-1, and NF-AT. These transcription factors are
important for T cell survival, activation, and differentiation. Phosphorylation of PKC-θ at …
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 immunological synapse, leading to activation of NF-κB, AP-1, and NF-AT. These transcription factors are important for T cell survival, activation, and differentiation. Phosphorylation of PKC-θ at multiple Ser/Thr/Tyr residues is induced in T cells during TCR 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 during TCR signaling.
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