title: Phosphatidylinositol 3-phosphate-binding protein AtPH1 controls the localization of the metal transporter NRAMP1 inArabidopsis.
abstract: "Too much of a good thing" perfectly describes the dilemma that living organisms face with metals. The tight control of metal homeostasis in cells depends on the trafficking of metal transporters between membranes of different compartments. However, the mechanisms regulating the location of transport proteins are still largely unknown. DevelopingArabidopsis thalianaseedlings require the natural resistance-associated macrophage proteins (NRAMP3 and NRAMP4) transporters to remobilize iron from seed vacuolar stores and thereby acquire photosynthetic competence. Here, we report that mutations in the pleckstrin homology (PH) domain-containing protein AtPH1 rescue the iron-deficient phenotype ofnramp3nramp4Our results indicate that AtPH1 binds phosphatidylinositol 3-phosphate (PI3P) in vivo and acts in the late endosome compartment. We further show that loss of AtPH1 function leads to the mislocalization of the metal uptake transporter NRAMP1 to the vacuole, providing a rationale for the reversion ofnramp3nramp4phenotypes. This work identifies a PH domain protein as a regulator of plant metal transporter localization, providing evidence that PH domain proteins may be effectors of PI3P for protein sorting.
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
authors.forename: Astrid
authors.initials: A
authors.lastname: Agorio
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
authors.forename: Jérôme
authors.initials: J
authors.lastname: Giraudat
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.|Unité de Formation et de Recherche Sciences et Technologie, Université Paris-Est Créteil Val de Marne, 94010 Créteil, France.
authors.forename: Michele Wolfe
authors.initials: MW
authors.lastname: Bianchi
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
authors.forename: Jessica
authors.initials: J
authors.lastname: Marion
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
authors.forename: Christelle
authors.initials: C
authors.lastname: Espagne
authors.affiliation: Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, CNRS, UMR 5004, Institut de Biologie Intégrative des Plantes, Montpellier, France.
authors.forename: Loren
authors.initials: L
authors.lastname: Castaings
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France.
authors.forename: Françoise
authors.initials: F
authors.lastname: Lelièvre
authors.affiliation: Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, CNRS, UMR 5004, Institut de Biologie Intégrative des Plantes, Montpellier, France.
authors.forename: Catherine
authors.initials: C
authors.lastname: Curie
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France; sylvain.merlot@i2bc.paris-saclay.fr sebastien.thomine@i2bc.paris-saclay.fr.
authors.forename: Sébastien
authors.initials: S
authors.lastname: Thomine
authors.affiliation: Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette cedex, France; sylvain.merlot@i2bc.paris-saclay.fr sebastien.thomine@i2bc.paris-saclay.fr.
authors.forename: Sylvain
authors.identifier: 0000-0002-9352-1184
authors.initials: S
authors.lastname: Merlot
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000254:growth & development / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D001483:Base Sequence; D027682:Cation Transport Proteins / Q000378:metabolism*; D017136:Ion Transport; D008670:Metals / Q000378:metabolism*; D009154:Mutation; D010641:Phenotype; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism*; D018517:Plant Roots / Q000254:growth & development / Q000378:metabolism*; D000099173:Natural Resistance-associated Macrophage Protein 1
chemical_list: D029681:Arabidopsis Proteins; D027682:Cation Transport Proteins; D008670:Metals; D018129:Phosphatidylinositol Phosphates; D000099173:Natural Resistance-associated Macrophage Protein 1; C055525:phosphatidylinositol 3-phosphate
keywords: NRAMP; late endosome; metal transport; phosphatidylinositol 3-phosphate; vacuole