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

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 are known to control the turnover of ph...

Full description

Saved in:
Bibliographic Details
Published inbioRxiv
Main Authors Ito, Yoko, Esnay, Nicolas, Platre, Matthieu Pierre, Noack, Lise C, Menzel, Wilhelm, Claverol, Stéphane, Moreau, Patrick, Jaillais, Yvon, Boutté, Yohann
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 14.05.2020
Subjects
Endoplasmic reticulum
Golgi apparatus
Homeostasis
Lipid composition
Lipids
Organelles
Phosphoinositides
Phospholipase C
Plant cells
Protein transport
Sphingolipids
Online AccessGet full text

Cover

More Information
Summary: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 are known to control the turnover of phosphoinositides through lipid exchange mechanisms at endoplasmic reticulum/TGN contact sites. In this study, we discovered a completely new mechanism acting on sphingolipid-mediated phosphoinositides homeostasis at the TGN in plant cells. We used multi-approaches to show that a reduction of the acyl-chain length of sphingolipid results in increased level of phosphatidylinositol-4-phosphate (PI4P) at the TGN, independently from either lipid exchange induced by sphingolipid synthetic flux, or local PI4P synthesis. Instead, we found that sphingolipids mediate the consumption of PI4P through phosphoinositide-specific phospholipase C (PI-PLC) and this process impacts the sorting of the auxin efflux carrier PIN2 at the TGN. Together, our data identify a new mode of action of sphingolipids in lipid interplay at the TGN during protein sorting. Competing Interest Statement The authors have declared no competing interest.
DOI:10.1101/2020.05.12.090399