4.6 Review

Plant phospholipases D and C and their diverse functions in stress responses

Journal

PROGRESS IN LIPID RESEARCH
Volume 62, Issue -, Pages 55-74

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.plipres.2016.01.002

Keywords

PLD; PLC; PA; DAG; IP3; IP6; Vesicular trafficking; Cytoskeleton; Lipid-protein interaction; Hormone signaling; Plant-pathogen interaction; Defense response; Membrane remodeling; Lipid hydrolysis

Funding

  1. US National Science Foundation [105-0818740, MCB-0922879]
  2. US Department of Agriculture [2007-35318-18393, 2016-67013-24429]
  3. US Department of Energy [DE-SC0001295, DE-AR0000202]
  4. National Natural Science Foundation of China [31470762, 30871303, 31271514]
  5. Chinese National Key Basic Research Project [2012CB114200]
  6. Major State Basic Research Development Program of China [20130127001]
  7. Fundamental Research Funds for the Central Universities [2013PY065, 2662015PY090]

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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. (C) 2016 Published by Elsevier Ltd.

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