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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Casein Kinase 2 interacts with human mitogen- and stress-activated protein kinase MSK1 and phosphorylates it at Multiple sites

  • Shi, Yan (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Han, Guanghui (CAS Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic R&A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences) ;
  • Wu, Huiling (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Ye, Kan (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Tian, Zhipeng (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Wang, Jiaqi (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Shi, Huili (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University) ;
  • Ye, Mingliang (CAS Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic R&A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences) ;
  • Zou, Hanfa (CAS Key Laboratory of Separation Science for Analytical Chemistry, National Chromatographic R&A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences) ;
  • Huo, Keke (State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University)
  • Published : 2009.12.31
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Abstract

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 p38$\alpha$. 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 CK2$\beta$ regulatory subunit of CK2. Interactions between MSK1 and the CK2$\alpha$ catalytic subunit and CK2$\beta$ subunit were demonstrated in vitro and in vivo. We further found that CK2$\alpha$ 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.

Keywords

References

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