Protein kinase CK2 phosphorylates BAD at threonine-117

Neurochemistry International
Susanne KlumppJosef Krieglstein

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.

Citations

Feb 15, 2011·The Journal of Biological Chemistry·Lisa PolzienUlf R Rapp
Jun 30, 2009·Antioxidants & Redox Signaling·Gillian GroegerThomas G Cotter
Jan 1, 2009·Research Letters in Biochemistry·Marie-Christin ThissenSusanne Klumpp
Mar 29, 2008·Cancer Letters·J S ClerkinT G Cotter
Mar 6, 2007·Advances in Enzyme Regulation·Ulf R RappStefan Albert
Aug 23, 2011·Biochimica Et Biophysica Acta·Mehdi Mollapour, Len Neckers
Jan 13, 2012·Journal of Proteomics·Viviane C H da Silva, Carlos H I Ramos
Jan 28, 2005·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Mary Ellen K Olsten, David W Litchfield
Jul 20, 2019·Artificial Cells, Nanomedicine, and Biotechnology·Hao ZhuQiang Shen
Apr 20, 2010·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Miriam López-RamosClaude Cochet
Nov 1, 2006·Biochemical Society Transactions·S KlumppJ Krieglstein
Feb 13, 2008·Molecular and Cellular Biochemistry·Maciej MasłykRyszard Szyszka

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