AtPH1 protein
; carrier protein
; natural resistance associated macrophage protein 1
; phosphate binding protein
; phosphatidylinositol 3 phosphate
; unclassified drug
; Arabidopsis protein
; cation transport protein
; metal
; natural resistance-associated macrophage protein 1
; phosphatidylinositol 3 phosphate
; polyphosphoinositide
; Arabidopsis thaliana
; Article
; controlled study
; in vivo study
; nonhuman
; pleckstrin homology domain
; priority journal
; protein depletion
; protein lipid interaction
; protein localization
; seedling
; amino acid sequence
; Arabidopsis
; growth, development and aging
; ion transport
; metabolism
; mutation
; nucleotide sequence
; phenotype
; plant root
; Amino Acid Sequence
; Arabidopsis
; Arabidopsis Proteins
; Base Sequence
; Cation Transport Proteins
; Ion Transport
; Metals
; Mutation
; Phenotype
; Phosphatidylinositol Phosphates
; Plant Roots
英文摘要:
"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. Developing Arabidopsis thaliana seedlings 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 of nramp3nramp4. Our 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 of nramp3nramp4 phenotypes. 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.
Agorio, A., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Giraudat, J., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Bianchi, M.W., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France, Unité de Formation et de Recherche Sciences et Technologie, Université Paris-Est Créteil Val de Marne, réteil, 94010, C, France; Marion, J., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Espagne, C., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Castaings, L., Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, Montpellier, France; Lelièvre, F., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Curie, C., Laboratoire de Biochimie et Physiologie Moléculaire des Plantes, Institut de Biologie Intégrative des Plantes, Montpellier, France; Thomine, S., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France; Merlot, S., Institute for Integrative Biology of Cell (I2BC), Université Paris-Sud, cedex, 91198, France
Recommended Citation:
Agorio A.,Giraudat J.,Bianchi M.W.,et al. Phosphatidylinositol 3-phosphate-binding protein AtPH1 controls the localization of the metal transporter NRAMP1 in Arabidopsis[J]. Proceedings of the National Academy of Sciences of the United States of America,2017-01-01,114(16)