Regulation of PKC-θ Function by Phosphorylation in T Cell Receptor Signaling

Overview

Journal Front Immunol

Specialty Allergy & Immunology

Date 2012 Jul 17

PMID 22798961

Citations 38

Authors

Xiaohong Wang

Huai-Chia Chuang

Ju-Pi Li

Tse-Hua Tan

Affiliations

Soon will be listed here.

Abstract

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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