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Significance Ser/Thr phosphorylation is critical for T cell receptor signal transduction as well as cell survival/death regulation in developing thymocytes. In this work, we established a Ser/Thr phosphorylation profile during thymocytes selection. Substrate analysis revealed PP2A as the most important enzyme responsible for the dephosphorylation events, which was proved in the PP2A cKO model. Thymic-specific depletion of PP2A caused impaired thymocyte selection. The decrease of DP thymocytes upon PP2A cKO is accompanied by dysregulated dephosphorylation of apoptosis-related proteins and increased cell apoptosis, which could be rescued by Bcl2 transgene or p53 knockout. This studies the role of PP2A in thymocyte development and provides insights to understand T cell development through dephosphorylation regulation of apoptosis-related molecules.

Protein phosphatase 2A has an essential role in promoting thymocyte survival during selection