Osmotic Stress Activates Two Reactive Oxygen Species Pathways with Distinct Effects on Protein Nanodomains and Diffusion
| Autor: | Yvon Jaillais, Stéphane Mari, Jean-Bernard Fiche, Xavier Dumont, Marija Smokvarska, Alexandre Martinière, Christophe Maurel, Carine Alcon, Marcelo Nollmann, Kian Hématy |
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| Přispěvatelé: | Biochimie et Physiologie Moléculaire des Plantes (BPMP), Université de Montpellier (UM)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), Centre de Biochimie Structurale [Montpellier] (CBS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Reproduction et développement des plantes (RDP), École normale supérieure - Lyon (ENS Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Baracco, Chantal, Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS)-Centre international d'études supérieures en sciences agronomiques (Montpellier SupAgro)-Institut National de la Recherche Agronomique (INRA)-Institut national d’études supérieures agronomiques de Montpellier (Montpellier SupAgro), 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), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM) |
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
Osmotic shock Physiology [SDV]Life Sciences [q-bio] Arabidopsis Aquaporin Plant Science Aquaporins Endocytosis 01 natural sciences Protein Domains Osmotic Pressure Genetics [SDV.BV]Life Sciences [q-bio]/Vegetal Biology Arabidopsis thaliana [SDV.BV] Life Sciences [q-bio]/Vegetal Biology chemistry.chemical_classification Reactive oxygen species biology Arabidopsis Proteins Chemistry Cell Biology biology.organism_classification Cell biology [SDV] Life Sciences [q-bio] Second messenger system Signal transduction Reactive Oxygen Species Signal Transduction 010606 plant biology & botany |
| Zdroj: | Plant Physiology Plant Physiology, American Society of Plant Biologists, 2019, 179 (4), pp.1581-1593. ⟨10.1104/pp.18.01065⟩ Plant Physiology, 2019, 179 (4), pp.1581-1593. ⟨10.1104/pp.18.01065⟩ |
| ISSN: | 1532-2548 0032-0889 |
| Popis: | Physiological acclimation of plants to an everchanging environment is governed by complex combinatorial signaling networks that perceive and transduce various abiotic and biotic stimuli. Reactive oxygen species (ROS) serve as one of the second messengers in plant responses to hyperosmotic stress. The molecular bases of ROS production and the primary cellular processes that they target were investigated in the Arabidopsis (Arabidopsis thaliana) root. Combined pharmacological and genetic approaches showed that the RESPIRATORY BURST OXIDASE HOMOLOG (RBOH) pathway and an additional pathway involving apoplastic ascorbate and iron can account for ROS production upon hyperosmotic stimulation. The two pathways determine synergistically the rate of membrane internalization, within minutes after activation. Live superresolution microscopy revealed at single-molecule scale how ROS control specific diffusion and nano-organization of membrane cargo proteins. In particular, ROS generated by RBOHs initiated clustering of the PLASMA MEMBRANE INTRINSIC PROTEIN2;1 aquaporin and its removal from the plasma membrane. This process is contributed to by clathrin-mediated endocytosis, with a positive role of RBOH-dependent ROS, specifically under hyperosmotic stress. |
| Databáze: | OpenAIRE |
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