PKN regulates phospholipase D1 through direct interaction

Citation
K. Oishi et al., PKN regulates phospholipase D1 through direct interaction, J BIOL CHEM, 276(21), 2001, pp. 18096-18101
Citations number
39
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
0021-9258 → ACNP
Volume
276
Issue
21
Year of publication
2001
Pages
18096 - 18101
Database
ISI
SICI code
0021-9258(20010525)276:21<18096:PRPDTD>2.0.ZU;2-5
Abstract
The association of phospholipase (PLD)-1 with protein kinase C-related prot ein kinases, PKN alpha and PKN beta, was analyzed. PLD1 interacted with PKN alpha and PKN beta in COS-7 cells transiently transfected with PLD1 and PK N alpha or PKN beta expression constructs. The interactions between endogen ous PLD1 and PKN alpha or PKN beta were confirmed by co-immunoprecipitation from mammalian cells. In vitro binding studies using the deletion mutants of PLD1 indicated that PKN alpha directly bound to residues 228-598 of PLD1 and that PKN beta interacted with residues 1-228 and 228-598 of PLD1. PKN alpha stimulated the activity of PLD1 in the presence of phosphatidylinosit ol 4,5-bisphosphate in vitro, whereas PKN beta had a modest effect on the s timulation of PLD1 activity. The stimulation of PLD1 activity by PKN alpha was slightly enhanced by the addition of arachidonic acid. These results su ggest that the PKN family functions as a novel intracellular player of PLD1 signaling pathway.