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Updated: Aug 23, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
Protein kinase CK2 phosphorylates BAD at threonine-117
Susanne Klumpp1, Anette Mäurer, Yuan Zhu
1Institut für Pharmazeutische & Medizinische Chemie, Westfälische Wilhelms-Universität, Hittorfstr. 58-62, D-48149 Münster, Germany. klumpp@uni-muenster.de
Abstract:
Reversible phosphorylation of the 22 kDa BAD protein is crucial for cell survival. Five phosphorylation sites, all serines, had been identified. Here we report on number six. It is threonine-117 phosphorylated by the constitutively active kinase, CK2. Phosphoamino acid analysis and phospho-specific antibodies confirmed Thr117 as additional phosphorylation site. Immunoprecipitation furthermore revealed that BAD is phosphorylated at Thr117 in cultured cortical neurons. PP1, PP2A and PP2C dephosphorylated BAD at Thr117, but PP2B did not. The discovery of the constitutively active CK2 phosphorylating BAD is shedding an unexpected light in the otherwise strictly signal-regulated phosphorylation events on BAD.
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