Sphingolipids mediate polar sorting of PIN2 through phosphoinositide consumption at the trans-Golgi network

Yoko Ito, Nicolas Esnay, Matthieu Pierre Platre, Valérie Wattelet-Boyer, Lise C. Noack, Louise Fougère, Wilhelm Menzel, Stéphane Claverol, Laetitia Fouillen, Patrick Moreau, Yvon Jaillais and Yohann Boutté ()
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Yoko Ito: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Nicolas Esnay: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Matthieu Pierre Platre: Laboratoire Reproduction et Développement des Plantes, Université de Lyon, ENS de Lyon, UCB Lyon1, CNRS, INRAE
Valérie Wattelet-Boyer: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Lise C. Noack: Laboratoire Reproduction et Développement des Plantes, Université de Lyon, ENS de Lyon, UCB Lyon1, CNRS, INRAE
Louise Fougère: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Wilhelm Menzel: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Stéphane Claverol: Platforme Proteome, Univ. Bordeaux
Laetitia Fouillen: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Patrick Moreau: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux
Yvon Jaillais: Laboratoire Reproduction et Développement des Plantes, Université de Lyon, ENS de Lyon, UCB Lyon1, CNRS, INRAE
Yohann Boutté: Laboratoire de Biogenèse Membranaire, Univ. Bordeaux

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract The lipid composition of organelles acts as a landmark to define membrane identity and specify subcellular function. Phosphoinositides are anionic lipids acting in protein sorting and trafficking at the trans-Golgi network (TGN). In animal cells, sphingolipids control the turnover of phosphoinositides through lipid exchange mechanisms at endoplasmic reticulum/TGN contact sites. In this study, we discover a mechanism for how sphingolipids mediate phosphoinositide homeostasis at the TGN in plant cells. Using multiple approaches, we show that a reduction of the acyl-chain length of sphingolipids results in an increased level of phosphatidylinositol-4-phosphate (PtdIns(4)P or PI4P) at the TGN but not of other lipids usually coupled to PI4P during exchange mechanisms. We show that sphingolipids mediate Phospholipase C (PLC)-driven consumption of PI4P at the TGN rather than local PI4P synthesis and that this mechanism is involved in the polar sorting of the auxin efflux carrier PIN2 at the TGN. Together, our data identify a mode of action of sphingolipids in lipid interplay at the TGN during protein sorting.

Date: 2021
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DOI: 10.1038/s41467-021-24548-0

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