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Article Dans Une Revue eLife Année : 2017

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

Résumé

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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hal-01606735 , version 1 (26-05-2020)

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Julien Gronnier, Jean Marc Crowet, Birgit Habenstein, Mehmet Nail Nasir, Vincent Bayle, et al.. Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains. eLife, 2017, 6, ⟨10.7554/eLife.26404⟩. ⟨hal-01606735⟩
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