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Protein kinase CK2 phosphorylates BAD at threonine-117.

机译:蛋白激酶CK2使苏氨酸117处的BAD磷酸化。

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摘要

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.
机译:22 kDa BAD蛋白的可逆磷酸化对于细胞存活至关重要。已经鉴定出全部为丝氨酸的五个磷酸化位点。在这里,我们报告第六。它被组成型活性激酶CK2磷酸化的苏氨酸117。磷酸氨基酸分析和磷酸特异性抗体证实Thr117为额外的磷酸化位点。免疫沉淀进一步显示,在培养的皮层神经元中,BAD在Thr117处被磷酸化。 PP1,PP2A和PP2C在Thr117处使BAD磷酸化,而PP2B则没有。组成性活性CK2磷酸化BAD的发现使BAD上其他严格受信号调控的磷酸化事件中产生了意外光。

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