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Plant PLC-DGK/PA Pathway Mediated Osmotic Stress Response
Jia Xiaowei#, Jia Yangyang#, Si Xuyang, Pan Yanyun*
Key Laboratory of Hebei Province for Plant Physiology and Molecular Pathology, College of Life, Hebei Agricola University, Baoding 071000, China
Abstract: Phosphoinositide (PI)-specific phospholipase C (PLC) is one of the important component of the canonical PI signaling system. Stimulation activates PLC， which hydrolyses phosphatidylinositol 4，5-bisphosphate (PIP2) into two second messengers: inositol 1，4，5-trisphosphate (IP3) and diacylglycerol (DAG). DAG activated protein kinase C (PKC) by which regulate a wide variety of cellular functions in animals. Plant genomes lack homologues of the PKC. Instead， plants utilize the phosphatidic acid (PA)， phosphorylation products of DAG by diacylglycerol kinase (DGK)， as a new plant-specific second messengers. These enzymes and their reaction substrates and products play important and multifaceted roles in plant response to abiotic and biotic stresses. In this paper， we reviewed the role of plant PLC-DGK/PA pathway in response to osmotic stress based on the expression characteristics of PLC and DGK and the changes of lipid signal molecules. In addition to PLC-DG activity， PA can also be produced by phospholipase D (PLD)， and the actions of common and distinguishable among the different pathways will also be discussed.
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