Academic Journal
A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants
| العنوان: | A nanodomain-anchored scaffolding complex is required for the function and localization of phosphatidylinositol 4-kinase alpha in plants |
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| المؤلفون: | Noack, Lise, C, Bayle, Vincent, Armengot, Laia, Rozier, Frédérique, Mamode-Cassim, Adiilah, Stevens, Floris, D, Caillaud, Marie-Cécile, Munnik, Teun, Mongrand, Sébastien, Pleskot, Roman, Jaillais, Yvon |
| المساهمون: | Reproduction et développement des plantes (RDP), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Laboratoire de biogenèse membranaire (LBM), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Agroécologie Dijon, Université de Bourgogne (UB)-Université Bourgogne Franche-Comté COMUE (UBFC)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Swammerdam Institute for Life Sciences (SILS), University of Amsterdam Amsterdam = Universiteit van Amsterdam (UvA), Institute of Experimental Botany of the Czech Academy of Sciences (IEB / CAS), Czech Academy of Sciences Prague (CAS), Y.J. was funded by ERC no. 3363360-APPL under FP/2007-2013 and ANR caLIPSO (ANR18-CE13-0025), M.-C.C. by astart-up package “font de recherche – projet e´mergent”from ENS de Lyon, S.M. by project PlayMobil ANR-19-CE20-0016-02 and by project PhosphoREM-domain ANR-19-CE13-0021-01, L.C.N. by a PhD fellowship from the French Ministryof Higher Education, and R.P. by the Czech ScienceFoundation grant 19-21758S, ANR-18-CE13-0025,caLIPSO,Mécanismes du pattern lipidique du réseau trans-Golgien (trans-Golgi Network) et rôles dans le tri des protéines, la polarité cellulaire et le développement des plantes(2018), ANR-19-CE20-0016,PLAYMOBIL,Vers un modèle intégratif de la bicouche lipidique de la membrane plasmique végétale(2019), ANR-19-CE13-0021,PhosphoREM-domain,Régulation de la communication intercellulaire - le rôle de la phosphoprotéine REMORIN liée aux nanodomaines de la membrane plasmique(2019) |
| المصدر: | ISSN: 1040-4651. |
| بيانات النشر: | HAL CCSD American Society of Plant Biologists (ASPB) |
| سنة النشر: | 2022 |
| المجموعة: | HAL Lyon 1 (University Claude Bernard Lyon 1) |
| مصطلحات موضوعية: | [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology |
| الوصف: | International audience ; 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. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | hal-03330567; https://hal.science/hal-03330567; https://hal.science/hal-03330567v2/document; https://hal.science/hal-03330567v2/file/koab135.pdf; WOS: 000745840600018 |
| DOI: | 10.1093/plcell/koab135 |
| الاتاحة: | https://hal.science/hal-03330567 https://hal.science/hal-03330567v2/document https://hal.science/hal-03330567v2/file/koab135.pdf https://doi.org/10.1093/plcell/koab135 |
| Rights: | http://creativecommons.org/licenses/by/ ; info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.84ED2EB7 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1093/plcell/koab135 |
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