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KMID : 0624620090420120840
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BMB Reports
2009 Volume.42 No. 12 p.840 ~ p.845
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Casein Kinase 2 interacts with human mitogen- and stress-activated protein kinase MSK1 and phosphorylates it at Multiple sites
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Shi Yan
Wu Huiling
Ye Kan
Tian Zhipeng
Wang Jiaqi
Shi Huili
Huo Keke
Han Guanghui
Ye Mingliang
Zou Hanfa
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Abstract
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Mitogen- and stress-activated protein kinase (MSK1) palys a crucial role in the regulation of transcription downstream of extracellular-signal-regulated kinase1/2 (ERK1/2) and mitogen- activated protein kinase p38. MSK1 can be phosphorylated and activated in cells by both ERK1/2 and p38α. In this study, Casein Kinase 2 (CK2) was identified as a binding and regulatory partner for MSK1. Using the yeast two-hybrid system, MSK1 was found to interact with the CK2β regulatory subunit of CK2. Interactions between MSK1 and the CK2α catalytic subunit and CK2β subunit were demonstrated in vitro and in vivo. We further found that CK2α can only interact with the C-terminal kinase domain of MSK1. Using site-directed mutagenesis assay and mass spectrometry, we identified five sites in the MSK1 C-terminus that could be phosphorylated by CK2 in vitro: Ser757, Ser758, Ser759, Ser760 and Thr793. Of these, Ser757, Ser759, Ser760 and Thr793 were previously unknown.
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KEYWORD
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CK2, Mass spectrometry, MSK1, Phosphorylation, Yeast two-hybrid
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