4.5 Article

Protein kinase CK2 phosphorylates BAD at threonine-117

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NEUROCHEMISTRY INTERNATIONAL
卷 45, 期 5, 页码 747-752

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PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.neuint.2004.02.006

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BAD; kinases; phosphatases; protein kinase CK2; signal transduction

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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. (C) 2004 Elsevier Ltd. All rights reserved.

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