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Updated: May 19, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Eat in or take away? How phosphatidylinositol 4-kinases feed the phospholipase C pathway with substrate
Elise Delage1, Eric Ruelland, Alain Zachowski
1Université Pierre et Marie Curie (Paris VI), CNRS, EAC7180, UR5 Physiologie Cellulaire et Moléculaire des Plantes, Paris, France.
Abstract:
Phosphatidylinositol 4-kinases (PI4Ks) catalyze the first step in the synthesis of phosphoinositide pools hydrolysed by phosphoinositide-dependent phospholipase C (PI-PLC) and thus constitute a potential key regulation point of this pathway. Twelve putative PI4K isoforms, divided as type-II (AtPI4KIIγ1- 8) and type-III PI4Ks (AtPI4KIIIα1- 2 and AtPI4KIIIβ1- 2), have been identified in Arabidopsis genome. By a combination of pharmalogical and genetic approaches we recently evidenced that AtPI4KIIIβ1 and AtPI4KIIIβ2 contribute to supply PI-PLC with substrate and that AtPI4KIIIα1 is probably also involved in this process. Given the current knowledge on PI-PLC and type-III PI4Ks localization in plant cells it raises the question whether type-III PI4Ks produce phosphatidylinositol 4-phosphate at the site of its consumption by the PI-PLC pathway. We therefore discuss the spatial organization of substrate supply to PI-PLC in plant cells with reference to recent data evidenced in mammalian cells.
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