Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil interface plays crucial role in metal homeostasis.
In plants, the controlled absorption of soil nutrients by root epidermal cells is critical for growth and development. IRON-REGULATED TRANSPORTER 1 (IRT1) is the main root transporter taking up iron from the soil and is also the main entry route in plants for potentially toxic metals such as manganese, zinc, cobalt, and cadmium. Previous work demonstrated that the IRT1 protein localizes to early endosomes/trans-Golgi network (EE/TGN) and is constitutively endocytosed through a monoubiquitin- and clathrin-dependent mechanism. Here, we show that the availability of secondary non-iron metal substrates of IRT1 (Zn, Mn, and Co) controls the localization of IRT1 between the outer polar domain of the plasma membrane and EE/TGN in root epidermal cells. We also identify FYVE1, a phosphatidylinositol-3-phosphate-binding protein recruited to late endosomes, as an important regulator of IRT1-dependent metal transport and metal homeostasis in plants. FYVE1 controls IRT1 recycling to the plasma membrane and impacts the polar delivery of this transporter to the outer plasma membrane domain. This work establishes a functional link between the dynamics and the lateral polarity of IRT1 and the transport of its substrates, and identifies a molecular mechanism driving polar localization of a cell surface protein in plants.
Department of Plant Molecular Biology, Biophore Building, UNIL-Sorge, Université de Lausanne, 1015 Lausanne, Switzerland;
Marie
M
Barberon
Institut des Sciences du Végétal, Unité Propre de Recherche 2355, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France; and.
Guillaume
G
Dubeaux
Department of Plant Systems Biology, Technische Universität München, 85354 Freising, Germany.
Cornelia
C
Kolb
Department of Plant Systems Biology, Technische Universität München, 85354 Freising, Germany.
Erika
E
Isono
Institut des Sciences du Végétal, Unité Propre de Recherche 2355, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France; and.
Enric
E
Zelazny
Institut des Sciences du Végétal, Unité Propre de Recherche 2355, Centre National de la Recherche Scientifique, 91190 Gif-sur-Yvette, France; and gregory.vert@isv.cnrs-gif.fr.
Grégory
G
Vert
D017360:Arabidopsis / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology; D027682:Cation Transport Proteins / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity / Q000502:physiology*; D006706:Homeostasis / Q000502:physiology; D007501:Iron / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D057146:Multivesicular Bodies / Q000378:metabolism; D010641:Phenotype; D018517:Plant Roots / Q000166:cytology / Q000378:metabolism*; D030821:Plants, Genetically Modified; D012987:Soil; D020798:Two-Hybrid System Techniques
D029681:Arabidopsis Proteins; D027682:Cation Transport Proteins; C099651:IRT1 protein, Arabidopsis; D008670:Metals; D012987:Soil; D007501:Iron
Arabidopsis; PI3P; endocytosis; nutrition; radial transport