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J. Biol. Chem., Vol. 276, Issue 21, 18096-18101, May 25, 2001

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PKN Regulates Phospholipase D1 through Direct Interaction^*

Kumiko Oishi, Mikiko Takahashi^§, Hideyuki Mukai^§, Yoshiko Banno^¶, Shigeru Nakashima^¶, Yasunori Kanaho, Yoshinori Nozawa^**, and Yoshitaka Ono^§

From the  Graduate School of Science and Technology, and the ^§ Biosignal Research Center, Kobe University, Kobe 657-8501, Japan, the ^¶ Department of Biochemistry, Gifu University School of Medicine, Gifu 500-8076, Japan, the  Department of Pharmacology, Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, Japan, and the ^** Department of Environmental Cell Responses, Gifu International Institute of Biotechnology and Institute of Applied Biochemistry, Mitake, Gifu 505-0116, Japan

The association of phospholipase (PLD)-1 with protein kinase C-related protein kinases, PKN and PKN, was analyzed. PLD1 interacted with PKN and PKN in COS-7 cells transiently transfected with PLD1 and PKN or PKN expression constructs. The interactions between endogenous PLD1 and PKN or PKN were confirmed by co-immunoprecipitation from mammalian cells. In vitro binding studies using the deletion mutants of PLD1 indicated that PKN directly bound to residues 228-598 of PLD1 and that PKN interacted with residues 1-228 and 228-598 of PLD1. PKN stimulated the activity of PLD1 in the presence of phosphatidylinositol 4,5-bisphosphate in vitro, whereas PKN had a modest effect on the stimulation of PLD1 activity. The stimulation of PLD1 activity by PKN was slightly enhanced by the addition of arachidonic acid. These results suggest that the PKN family functions as a novel intracellular player of PLD1 signaling pathway.

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