| Literature DB >> 26783886 |
Yueyun Hong1, Jian Zhao2, Liang Guo3, Sang-Chul Kim4, Xianjun Deng5, Geliang Wang4, Gaoyang Zhang5, Maoyin Li4, Xuemin Wang6.
Abstract
Phospholipases D (PLD) and C (PLC) hydrolyze the phosphodiesteric linkages of the head group of membrane phospholipids. PLDs and PLCs in plants occur in different forms: the calcium-dependent phospholipid binding domain-containing PLDs (C2-PLDs), the plekstrin homology and phox homology domain-containing PLDs (PX/PH-PLDs), phosphoinositide-specific PLC (PI-PLC), and non-specific PLC (NPC). They differ in structures, substrate selectivities, cofactor requirements, and/or reaction conditions. These enzymes and their reaction products, such as phosphatidic acid (PA), diacylglycerol (DAG), and inositol polyphosphates, play important, multifaceted roles in plant response to abiotic and biotic stresses. Here, we review biochemical properties, cellular effects, and physiological functions of PLDs and PLCs, particularly in the context of their roles in stress response along with advances made on the role of PA and DAG in cell signaling in plants. The mechanism of actions, including those common and distinguishable among different PLDs and PLCs, will also be discussed.Entities:
Keywords: Cytoskeleton; DAG; Defense response; Hormone signaling; IP(3); IP(6); Lipid hydrolysis; Lipid−protein interaction; Membrane remodeling; PA; PLC; PLD; Plant−pathogen interaction; Vesicular trafficking
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Year: 2016 PMID: 26783886 DOI: 10.1016/j.plipres.2016.01.002
Source DB: PubMed Journal: Prog Lipid Res ISSN: 0163-7827 Impact factor: 16.195