Plant PA signaling via diacylglycerol kinase

被引:207
作者
Arisz, Steven A. [1 ]
Testerink, Christa [1 ]
Munnik, Teun [1 ]
机构
[1] Univ Amsterdam, Sect Plant Physiol, Swammerdam Inst Life Sci, NL-1098 XH Amsterdam, Netherlands
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2009年 / 1791卷 / 09期
关键词
Phosphatidic acid; Diacylglycerol kinase; Lipid signaling; Plant stress; Phospholipase; PHOSPHATIDIC-ACID ACCUMULATION; PHOSPHOLIPASE-D; PLASMA-MEMBRANE; PROTEIN-KINASE; ARABIDOPSIS-THALIANA; DISEASE RESISTANCE; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; SUSPENSION-CULTURE; FREEZING TOLERANCE; EARLY RESPONSE;
D O I
10.1016/j.bbalip.2009.04.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Accumulating evidence suggests that phosphatidic acid (PA) plays a pivotal role in the plant's response to environmental signals. Besides phospholipase D (PLD) activity, PA can also be generated by diacylglycerol kinase (DGK). To establish which metabolic route is activated, a differential P-32-radiolabelling protocol can be used. Based on this, and more recently on reverse-genetic approaches, DGK has taken center stage, next to PLD, as a generator of PA in biotic and abiotic stress responses. The DAG substrate is generally thought to be derived from PI-PLC activity. The model plant system Arabidopsis thaliana has 7 DGK isozymes, two of which, AtDGK1 and AtDGK2, resemble mammalian DGK epsilon, containing a conserved kinase domain, a transmembrane domain and two C1 domains. The other ones have a much simpler structure, lacking the C1 domains, not matched in animals. Several protein targets have now been discovered that bind PA. Whether the PA molecules engaged in these interactions come from PLD or DGK remains to be elucidated. (C) 2009 Elsevier B.V. All rights reserved.
引用
收藏
页码:869 / 875
页数:7
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