An extra sugar protects: Many microbial pathogens produce proteins that are toxic to the cells that they are targeting. Broad-leaved plants are susceptible to NLP (necrosis and ethylene-inducing peptide 1–like protein) toxins. Lenarčič et al. identified the receptors for NLP toxins to be GIPC (glycosylinositol phosphorylceramide) sphingolipids (see the Perspective by Van den Ackerveken). Their findings reveal why these toxins only attack broad-leaved plants (so-called eudicots): If the sphingolipid carries just two hexoses, as is the case for eudicots, the toxin binds and causes cell lysis. But in monocots with sphingolipids that have three hexoses, the toxin is ineffective. Science , this issue p. 1431 ; see also p. 1383

Lipid composition of plasma membrane (PM) and the corresponding Detergent-Insoluble Membrane (DIM) fraction were analyzed with a specific focus on highly polar sphingolipids so-called Glycosyl-Inositol-Phosphoryl-Ceramides (GIPCs). Using tobacco Bright Yellow-2 cell suspension and tobacco leaves (Nicotiana tabacum), evidences were provided that GIPCs represent up to 40 mol% of the PM lipids. Comparative analysis of DIMs with the PM showed an enrichment of 2-hydroxylated Very Long Chain Fatty Acid (VLCFA)-containing GIPCs and polyglycosylated GIPCs in the DIMs. Purified antibodies raised against these GIPCs were further used for immunogold-electron microscopy strategy, revealing the distribution of polyglycosylated GIPCs in domains of 35{plus minus}7nm in the plane of the PM. Biophysical studies also showed strong interactions between GIPCs and sterols, and suggested a role for VLCFA in the interdigitation between the two PM composing-monolayers. The ins and outs of lipid asymmetry, raft formation and interdigitation in plant membrane biology are finally discussed.

Plasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORINis independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyzes of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.