Abstract
Many signaling proteins permanently or transiently localize to specific organelles for function. 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 (PI4P). Our results further reveal that, contrarily to other eukaryotes, PI4P 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 REGULATORs (MAKRs) family, which are involved in brassinosteroid and receptor-like kinase signaling. We anticipate that this PI4P-driven physical membrane property will control the localization and function of many proteins involved in development, reproduction, immunity and nutrition.
Highlights
Many signaling proteins permanently or transiently localize to specific organelles for function
We found that mutants impaired in PI4P binding did not localized at the plasma membrane (PM) but in the cytosol as well as endomembranes, likely because of binding to ARF1 (Fig. 3l–m)
In this study we found that PI4P biosensors accumulate at the PM in various cell types and in two plant species (i.e. Arabidopsis thaliana and Nicotiana benthamiana)
Summary
Many signaling proteins permanently or transiently localize to specific organelles for function. It is well established that certain lipids act as biochemical landmarks to specify compartment identity They influence membrane biophysical properties, which emerge as important features in specifying cellular territories. 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 REGULATORs (MAKRs) family, which are involved in brassinosteroid and receptor-like kinase signaling. Our results further revealed that the specific electrostatic field of the PM is lost upon chemical or genetic depletion of PI4P and that it contributes to the PM localization and function of several proteins involved in hormone and receptor-like kinase signaling
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