Regulation of phospholipase C isozymes: Activation of phospholipase C-γ in the absence of tyrosine-phosphorylation

Fujio Sekiya, Yun Soo Bae, Sue Goo Rhee

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

Abstract

Activation of PLC-γ isozymes in response to various agonists involves tyrosine phosphorylation of the effector enzymes. Recent evidence indicates that PLC-γ isozymes are additionally activated by phosphatidic acid, phosphatidylinositol 3,4,5-trisphosphate and arachidonic acid in the absence of PLC-γ tyrosine phosphorylation. These lipid-derived messengers are the immediate products of phospholipase D, phosphatidylinositol 3-kinase, and phospholipase A2, enzymes which are often stimulated along with PLC-γ in response to an agonist. Furthermore, phosphatidylinositol 4,5-bisphosphate acts as a substrate for both PLC-γ and phosphatidylinositol 3-kinase and as an activator for phospholipase D and phospholipase A2. These results reveal an elaborate mechanism of cross-talk and mutual regulation between four effector enzymes that participate in receptor signaling by acting on phospholipids. Copyright (C) 1999 Elsevier Science Ireland Ltd.

Original languageEnglish
Pages (from-to)3-11
Number of pages9
JournalChemistry and Physics of Lipids
Volume98
Issue number1-2
DOIs
StatePublished - Apr 1999

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