Carbachol-induced Phosphorylation of Phospholipase D1 through Protein Kinase C is required for the Activation in COS-7 cells

Byoung Dae Lee, Yong Kim, Jung Min Han, Pann Ghill Suh, Sung Ho Ryu

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Phospholiapse D (PLD), and phosphatidic acid generated by it, have been implicated in receptor-mediated intracellular signaling. Carbachol (CCh) is known to activate PLD1, and protein kinase C (PKC) is known to mediate in this signaling pathway. In recent reports (Kim et al., 1999b; Kim et al., 2000), we published our observations of the direct phosphorylation of PLD1 by PKC and we described the phosphorylation-dependent regulation of PLD1 activity. In this study, we investigated the phosphorylation and compartmentalization of PLD1 in terms of CCh signaling in M3 muscarinic receptor (M3R)-expressing COS-7 cells. CCh treatment of COS-7 cells transiently co-expressing PLD1 and M3R stimulated PLD1 activity and induced direct phosphorylation of PLD1 by PKC. The CCh-induced activation and phosphorylation of PLD1 was completely blocked upon pretreatment of the cells with PKC-specific inhibitors. We looked at the localization of the PLD1 phosphorylation by PKC and found that PLD1 was mainly located in the caveolin-enriched membrane (CEM) fraction. Based on these results, we conclude that CCh induces the activation and phosphorylation of PLD1 via PKC and that the phosphorylation of PLD1 occurs in caveolae.

Original languageEnglish
Pages (from-to)182-187
Number of pages6
JournalJournal of Biochemistry and Molecular Biology
Volume34
Issue number2
Publication statusPublished - 2001 Mar 31

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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