植物磷酯酰肌醇特异性磷脂酶 C：深入了解
Plant phosphoinositide-specific phospholipase C: an insight.
机构信息
Department of Biochemistry, Indian Institute of Science, Bangalore, India.
出版信息
Plant Signal Behav. 2012 Oct 1;7(10):1281-3. doi: 10.4161/psb.21436. Epub 2012 Aug 20.
Abstract
Phosphoinositide-specific phospholipase C (PI-PLC) belongs to an important class of enzymes involved in signaling related to lipids. They hydrolyze a membrane-associated phospholipid, phosphatidylinositol-4,5-bisphosphate, to produce inositol-1,4,5-trisphosphate and diacylglycerol. The role of PI-PLC and the mechanism behind its functioning is well studied in animal system; however, mechanism of plant PI-PLC functioning remains largely obscure. Here, we attempted to summarize the understanding regarding plant PI-PLC mechanism of regulation, localization, and domain association. Using sedimentation based phospholipid binding assay and surface plasmon resonance spectroscopy, it was demonstrated that C2 domain of plant PI-PLC alone is capable of targeting membranes. Moreover, change in surface hydrophobicity upon calcium stimulus is the key element in targeting plant PI-PLC from soluble fractions to membranes. This property of altering surface hydrophobicity plays a pivot role in regulation of PI-PLC activity.
摘要
磷酸肌醇特异性磷脂酶 C（PI-PLC）属于一类重要的酶，参与与脂质相关的信号转导。它们水解膜相关磷脂酰肌醇-4,5-二磷酸，生成肌醇-1,4,5-三磷酸和二酰基甘油。PI-PLC 的作用及其作用机制在动物系统中得到了很好的研究；然而，植物 PI-PLC 作用的机制在很大程度上仍然不清楚。在这里，我们试图总结关于植物 PI-PLC 调节、定位和结构域关联机制的理解。通过基于沉淀的磷脂结合测定和表面等离子体共振光谱法，证明植物 PI-PLC 的 C2 结构域本身就能够靶向膜。此外，钙刺激引起的表面疏水性变化是将植物 PI-PLC 从可溶性部分靶向到膜的关键因素。这种改变表面疏水性的特性在调节 PI-PLC 活性中起着关键作用。
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