KMID : 0624620110440070490
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BMB Reports 2011 Volume.44 No. 7 p.490 ~ p.495
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CK2 phosphorylates AP-2¥á and increases its transcriptional activity
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Ren Kaiqun
Xiang Shuanglin He Fangli Zhang Wenfeng Ding Xiaofeng Wu Yanyang Yang Liping Zhou Jianlin Gao Xiang Zhang Jian
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Abstract
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Transcription factor AP-2¥á involves in the process of mammalian embryonic development and tumorigenesis. Many studies have shown that AP-2¥á functions in association with other interacting proteins. In a two-hybrid screening, the regulatory subunit ¥â of protein casein kinase 2 (CK2¥â) was identified as an interacting protein of AP-2¥á; we confirmed this interaction using in-vitro GST pull-down and in-vivo co-immunoprecipitation assays; in an endogenous co-immunoprecipitation experiment, we further found the catalytic subunit ¥á of protein casein kinase 2 (CK2¥á) also exists in the complex. Phosphorylation analysis revealed that AP-2¥á was phosphorylated by CK2 kinase majorly at the site of Ser429, and such phosphorylation could be blocked by CK2 specific inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) in a dose-dependent manner. Luciferase assays demonstrated that both CK2¥á and CK2¥â enhanced the transcription activity of AP-2¥á; moreover, CK2¥â increased the stability of AP-2¥á. Our data suggest a novel cellular function of CK-2 as a transcriptional co-activator of AP-2¥á.
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KEYWORD
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AP-2¥á, CK2, Phosphorylation, TBB, Transcription activity
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