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

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Gronnier, Julien | Crowet, Jean Marc | Habenstein, Birgit | Nasir, Mehmet Nail | Bayle, Vincent | Hosy, Eric | Platre, Matthieu Pierre | Gouguet, Paul | Raffaele, Sylvain | Martinez, Denis | Grelard, Axelle | Loquet, Antoine | Simon-Plas, Françoise | Gerbeau-Pissot, Patricia | Der, Christopher | Bayer, Emmanuelle M. | Jaillais, Yvon | Deleu, Magali | Germain, Véronique | Lins, Laurence | Mongrand, Sébastien

Edité par CCSD ; eLife Sciences Publication -

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.

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