ArticleJournal of cell science2015
Dictyostelium Nramp1, which is structurally and functionally similar to mammalian DMT1 transporter, mediates phagosomal iron efflux.
Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Metal Ions Within the Neuro-Immune-Tumor Axis.Journal of immunology research · 2026Review
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- Review
- Quantitative Analysis of the Inactivation Process of Internalized Bacteria in Dictyostelium Cells.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Legionella- and host-driven lipid flux at LCV-ER membrane contact sites promotes vacuole remodeling.EMBO reports · 2023Article
- The "www" ofMembranes · 2022Review
- Functional characterization of Atlantic salmon (Salmo salar L.) PepT2 transporters.The Journal of physiology · 2022Article
- Nramp: Deprive and conquer?Frontiers in cell and developmental biology · 2022Article
- Molecular Mechanism of Nramp-Family Transition Metal Transport.Journal of molecular biology · 2021Review
- ZnmBio · 2021Article
- Unique structural features in an Nramp metal transporter impart substrate-specific proton cotransport and a kinetic bias to favor import.The Journal of general physiology · 2019Article
- Iron oxide nanoparticles can cross plasma membranes.Scientific reports · 2017Article
- Metal homeostasis and resistance in bacteria.Nature reviews. Microbiology · 2017Review
- Article
- Eat Prey, Live:Frontiers in immunology · 2017Review
- Differential Effects of Iron, Zinc, and Copper onFrontiers in cellular and infection microbiology · 2017Article
- Nramp1 and NrampB Contribute to Resistance againstFrontiers in cellular and infection microbiology · 2017Article
- Cobalt oxide nanoparticles can enter inside the cells by crossing plasma membranes.Scientific reports · 2016Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Nramp (Slc11) protein family is widespread in bacteria and eukaryotes, and mediates transport of divalent metals across cellular membranes. The social amoeba Dictyostelium discoideum has two Nramp proteins. Nramp1, like its mammalian ortholog (SLC11A1), is recruited to phagosomal and macropinosomal membranes, and confers resistance to pathogenic bacteria. Nramp2 is located exclusively in the contractile vacuole membrane and controls, synergistically with Nramp1, iron homeostasis. It has long been debated whether mammalian Nramp1 mediates iron import or export from phagosomes. By selectively loading the iron-chelating fluorochrome calcein in macropinosomes, we show that Dictyostelium Nramp1 mediates iron efflux from macropinosomes in vivo. To gain insight in ion selectivity and the transport mechanism, the proteins were expressed in Xenopus oocytes. Using a novel assay with calcein, and electrophysiological and radiochemical assays, we show that Nramp1, similar to rat DMT1 (also known as SLC11A2), transports Fe(2+) and manganese, not Fe(3+) or copper. Metal ion transport is electrogenic and proton dependent. By contrast, Nramp2 transports only Fe(2+) in a non-electrogenic and proton-independent way. These differences reflect evolutionary divergence of the prototypical Nramp2 protein sequence compared to the archetypical Nramp1 and DMT1 proteins.
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