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Eat in or take away? How phosphatidylinositol 4-kinases feed the phospholipase C pathway with substrate.

Authors
  • Delage, Elise
  • Ruelland, Eric
  • Zachowski, Alain
  • Puyaubert, Juliette
Type
Published Article
Journal
Plant Signaling & Behavior
Publisher
Landes Bioscience
Publication Date
Sep 01, 2012
Volume
7
Issue
9
Pages
1197–1199
Identifiers
DOI: 10.4161/psb.21305
PMID: 22899063
Source
Medline
License
Unknown

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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