PKN Regulates Phospholipase D1 through Direct Interaction

The association of phospholipase (PLD)-1 with protein kinase C-related protein kinases, PKNα and PKNβ, was analyzed. PLD1 interacted with PKNα and PKNβ in COS-7 cells transiently transfected with PLD1 and PKNα or PKNβ expression constructs. The interactions between endogenous PLD1 and PKNα or PKNβ w...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-05, Vol.276 (21), p.18096-18101
Main Authors: Oishi, Kumiko, Takahashi, Mikiko, Mukai, Hideyuki, Banno, Yoshiko, Nakashima, Shigeru, Kanaho, Yasunori, Nozawa, Yoshinori, Ono, Yoshitaka
Format: Article
Language:English
Subjects:
Animals
COS Cells
Enzyme Activation
HeLa Cells
Humans
Phospholipase D - genetics
Phospholipase D - metabolism
Protein Binding
Protein Kinase C
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Protein-Tyrosine Kinases - genetics
Protein-Tyrosine Kinases - metabolism
Signal Transduction
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Summary:The association of phospholipase (PLD)-1 with protein kinase C-related protein kinases, PKNα and PKNβ, was analyzed. PLD1 interacted with PKNα and PKNβ in COS-7 cells transiently transfected with PLD1 and PKNα or PKNβ expression constructs. The interactions between endogenous PLD1 and PKNα or PKNβ were confirmed by co-immunoprecipitation from mammalian cells.In vitro binding studies using the deletion mutants of PLD1 indicated that PKNα directly bound to residues 228–598 of PLD1 and that PKNβ interacted with residues 1–228 and 228–598 of PLD1. PKNα stimulated the activity of PLD1 in the presence of phosphatidylinositol 4,5-bisphosphate in vitro, whereas PKNβ had a modest effect on the stimulation of PLD1 activity. The stimulation of PLD1 activity by PKNα 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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M010646200