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Elife. 2017 Jul 31;6. pii: e26404. doi: 10.7554/eLife.26404.

Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains.

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Laboratoire de Biogenèse Membranaire (LBM), Unité Mixte de Recherche UMR 5200, CNRS, Université de Bordeaux, Bordeaux, France.
Laboratoire de Biophysique Moléculaire aux Interfaces, GX ABT, Université de Liège, Gembloux, Belgium.
Institute of Chemistry and Biology of Membranes and Nanoobjects (UMR5248 CBMN), CNRS, Université de Bordeaux, Institut Polytechnique Bordeaux, Pessac, France.
Laboratoire Reproduction et Développement des Plantes, Université de Lyon, ENS de Lyon, Université Claude Bernard Lyon 1, Lyon, France.
Interdisciplinary Institute for Neuroscience, CNRS, University of Bordeaux, Bordeaux, France.
LIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, France.
Agroécologie, AgroSup Dijon, INRA, Université Bourgogne Franche-Comté, F-21000 Dijon, ERL 6003 CNRS, Dijon, France.


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 REMORIN is 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. Analyses 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.


Membrane domain; Nicotiana benthamiana; membrane structure; phospholipids; plant biology; sterols; targeting

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