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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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PKD2 interacts with Lck and regulates NFAT activity in T cells

  • Li, Qing (Department of Life Science and Biotechnology, Shanghai Jiaotong University) ;
  • Sun, Xiaoqing (Shanghai Genomics, Inc. and Functional Genomics II of the Chinese National Human Genome Center) ;
  • Wu, Jun (Department of Life Science and Biotechnology, Shanghai Jiaotong University) ;
  • Lin, Zhixin (Department of Life Science and Biotechnology, Shanghai Jiaotong University) ;
  • Luo, Ying (Department of Life Science and Biotechnology, Shanghai Jiaotong University)
  • Published : 2009.01.31
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Abstract

Protein kinase D2 (PKD2) is a member of the PKD serine/threonine protein kinase family that has been implicated in the regulation of a variety of cellular processes including proliferation, survival, protein trafficking and immune response. In the present study, we report a novel interaction between PKD2 and Lck, a member of the Src tyrosine protein kinase family that is predominantly expressed in T cells. This interaction involved the C-terminal kinase domains of both PKD2 and Lck. Moreover, co-expression of Lck enhanced the tyrosine phosphorylation of PKD2 and increased its kinase activity. Finally, we report that PKD2 enhanced T cell receptor (TCR)-induced nuclear factor of T cell (NFAT) activity in Jurkat T cells. These results suggested that Lck regulated the activity of PKD2 by tyrosine phosphorylation, which in turn may have modulated the physiological functions of PKD2 during TCR-induced T cell activation.

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References

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