Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil interface plays crucial role in metal homeostasis

Détails

ID Serval
serval:BIB_AD6954FF9236
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Polarization of IRON-REGULATED TRANSPORTER 1 (IRT1) to the plant-soil interface plays crucial role in metal homeostasis
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur⸱e⸱s
Barberon M., Dubeaux G., Kolb C., Isono E., Zelazny E., Vert G.
ISSN
0027-8424 (Print)
1091-6490 (Electronic)
ISSN-L
0027-8424
Statut éditorial
Publié
Date de publication
2014
Peer-reviewed
Oui
Volume
111
Numéro
22
Pages
8293-8298
Langue
anglais
Notes
Publication types: Biological Sciences ; research-article Identifiant PubMed Central: PMC4050562
Résumé
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.
Mots-clé
Arabidopsis/cytology, Arabidopsis/genetics, Arabidopsis/metabolism, Arabidopsis Proteins/genetics, Arabidopsis Proteins/metabolism, Biological Transport/physiology, Cation Transport Proteins/genetics, Cation Transport Proteins/metabolism, Cell Membrane/metabolism, Cell Polarity/physiology, Homeostasis/physiology, Iron/metabolism, Metals/metabolism, Multivesicular Bodies/metabolism, Plant Roots/cytology, Plant Roots/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
11/07/2016 10:04
Dernière modification de la notice
20/08/2019 15:17
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