A PtdIns(4)P-driven electrostatic field controls cell membrane identity and signalling in plants

作者：Simon, Mathilde Laetitia Audrey; Platre, Matthieu Pierre; Marques-Bueno, Maria Mar; Armengot, Laia; Stanislas, Thomas; Bayle, Vincent; Caillaud, Marie-Cecile^*; Jaillais, Yvon^*

来源：Nature Plants, 2016, 2(7): 16089.

DOI：10.1038/NPLANTS.2016.89

• ROOT HAIR-CELLS
• PLASMA-MEMBRANE
• PHOSPHATIDYLINOSITOL 4-PHOSPHATE
• ARABIDOPSIS-THALIANA
• RECEPTOR ACTIVATION
• PROTEIN
• TRAFFICKING
• KINASES
• DOMAINS
• LIPIDS

Many signalling proteins permanently or transiently localize to specific organelles. It is well established that certain lipids act as biochemical landmarks to specify compartment identity. However, they also influence membrane biophysical properties, which emerge as important features in specifying cellular territories. Such parameters include the membrane inner surface potential, which varies according to the lipid composition of each organelle. Here, we found that the plant plasma membrane (PM) and the cell plate of dividing cells have a unique electrostatic signature controlled by phosphatidylinositol-4-phosphate (PtdIns(4)P). Our results further reveal that, contrarily to other eukaryotes, PtdIns(4)P massively accumulates at the PM, establishing it as a critical hallmark of this membrane in plants. Membrane surface charges control the PM localization and function of the polar auxin transport regulator PINOID as well as proteins from the BRI1 KINASE INHIBITOR1 (BKI1)/MEMBRANE ASSOCIATED KINASE REGULATOR (MAKR) family, which are involved in brassinosteroid and receptor-like kinase signalling. We anticipate that this PtdIns(4)P-driven physical membrane property will control the localization and function of many proteins involved in development, reproduction, immunity and nutrition.

• 出版日期2016-7