Details

Autor(en) / Beteiligte

• 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, Christophe
• Bayer, Emmanuelle M
• Jaillais, Yvon
• Deleu, Magali
• Germain, Véronique
• Lins, Laurence
• Mongrand, Sébastien

Titel

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

Ist Teil von

• eLife, 2017-07, Vol.6

Ort / Verlag

England: eLife Science Publications, Ltd

Erscheinungsjahr

2017

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.