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Article Info.
2009.01.31; 42(1) pp. 35~40
Title

PKD2 interacts with Lck and regulates NFAT activity in T cells  

Authors

Qing Li1, Xiaoqing Sun2, Jun Wu1,2,3, Zhixin Lin1 & Ying Luo1,2,3,*  

Institutions

1Department of Life Science and Biotechnology, Shanghai Jiaotong University, 1954 Huashan Road, Shanghai, 200030, China, 2Shanghai Genomics, Inc. and Functional Genomics of the Chinese National Human Genome Center, Zhangjiang Hi-Tech Park, Shanghai, 201203, China, 3GNI, 4-2-12 Toranomon, Tokyo, 1050001, Japan  

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. [BMB reports 2009; 42(1): 35-40]  

Keywords

AP-1, Lck, NFAT, PKD2, TCR