Protein kinase CK2 phosphorylates BAD at threonine-117

• Published in: Neurochemistry international Vol. 45; no. 5; pp. 747 - 752
• Main Authors: Klumpp, Susanne, Mäurer, Anette, Zhu, Yuan, Aichele, Dagmar, Pinna, Lorenzo A, Krieglstein, Josef
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01-10-2004; Elsevier
• Subjects: Adenosine Triphosphate - metabolism; Animals; BAD; bcl-Associated Death Protein; Biological and medical sciences; Blotting, Western; Carrier Proteins - metabolism; Casein Kinase II; Cells, Cultured; Cerebral Cortex - cytology; Cerebral Cortex - metabolism; Cyclic AMP-Dependent Protein Kinases - metabolism; Fundamental and applied biological sciences. Psychology; Indicators and Reagents; Kinases; Mitogen-Activated Protein Kinase Kinases - metabolism; Neurons - metabolism; Phosphatases; Phosphoamino Acids - metabolism; Phosphoprotein Phosphatases - metabolism; Phosphorylation; Precipitin Tests; Protein kinase CK2; Protein-Serine-Threonine Kinases - metabolism; Proto-Oncogene Proteins - metabolism; Proto-Oncogene Proteins c-akt; Rats; Signal transduction; Threonine - metabolism; Vertebrates: nervous system and sense organs; p70S6K; Phosphatases; Protein kinase CK2; BAD; JNK; KLH; PKB; PKA; GST; PKC; CK2; RSK; Kinases; Cdc2; PP1; BSA; Signal transduction; PAK; Threonine; Enzyme; Transferases; Phosphoric monoester hydrolases; Esterases; Kinase; Protein kinase; Hydrolases
• ISSN: 0197-0186; 1872-9754
• DOI: 10.1016/j.neuint.2004.02.006

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 Thr
117 as additional phosphorylation site. Immunoprecipitation furthermore revealed that BAD is phosphorylated at Thr
117 in cultured cortical neurons. PP1, PP2A and PP2C dephosphorylated BAD at Thr
117, 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.