Abstract:
: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.
journal_name
Elifejournal_title
eLifeauthors
Gronnier J,Crowet JM,Habenstein B,Nasir MN,Bayle V,Hosy E,Platre MP,Gouguet P,Raffaele S,Martinez D,Grelard A,Loquet A,Simon-Plas F,Gerbeau-Pissot P,Der C,Bayer EM,Jaillais Y,Deleu M,Germain V,Lins L,Mongrand Sdoi
10.7554/eLife.26404subject
Has Abstractpub_date
2017-07-31 00:00:00issn
2050-084Xpii
26404journal_volume
6pub_type
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