NOACK, Lise C; BAYLE, Vincent; ARMENGOT, Laia; ROZIER, Frederique; MAMODE CASSIM, Adiilah; STEVENS, Floris D; CAILLAUD, Marie-Cecile; MUNNIK, Teun; MONGRAND, Sebastien; PLESKOT, Roman; JAILLAIS, Yvon

doi:10.1093/plcell/koab135

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Article de revue

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The Plant Cell. 2022-01, vol. 34, n° 1, p. 302-332

Résumé en anglais

Phosphoinositides are low-abundant lipids that participate in the acquisition of membrane identity through their spatiotemporal enrichment in specific compartments. Phosphatidylinositol 4-phosphate (PI4P) accumulates at the plant plasma membrane driving its high electrostatic potential, and thereby facilitating interactions with polybasic regions of proteins. PI4Kα1 has been suggested to produce PI4P at the plasma membrane, but how it is recruited to this compartment is unknown. Here, we pin-point the mechanism that tethers Arabidopsis thaliana phosphatidylinositol 4-kinase alpha1 (PI4Kα1) to the plasma membrane via a nanodomain-anchored scaffolding complex. We established that PI4Kα1 is part of a complex composed of proteins from the NO-POLLEN-GERMINATION, EFR3-OF-PLANTS, and HYCCIN-CONTAINING families. Comprehensive knockout and knockdown strategies revealed that subunits of the PI4Kα1 complex are essential for pollen, embryonic, and post-embryonic development. We further found that the PI4Kα1 complex is immobilized in plasma membrane nanodomains. Using synthetic mis-targeting strategies, we demonstrate that a combination of lipid anchoring and scaffolding localizes PI4Kα1 to the plasma membrane, which is essential for its function. Together, this work opens perspectives on the mechanisms and function of plasma membrane nanopatterning by lipid kinases.< Réduire

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https://oskar-bordeaux.fr/handle/20.500.12278/136415

DOI

http://dx.doi.org/10.1093/plcell/koab135

Project ANR

Vers un modèle intégratif de la bicouche lipidique de la membrane plasmique végétale
Régulation de la communication intercellulaire - le rôle de la phosphoprotéine REMORIN liée aux nanodomaines de la membrane plasmique

Unités de recherche

Laboratoire de Biogenèse Membranaire (LBM) - UMR 5200

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A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants

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Résumé en anglais

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