ArticlePLoS biology2004
A spontaneous, recurrent mutation in divalent metal transporter-1 exposes a calcium entry pathway.
Article in PLoS biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 75 citations in OpenAlex.
- Structural basis for metal ion transport by the human SLC11 proteins DMT1 and NRAMP1.Nature communications · 2025Article
- Iron from the gut: the role of divalent metal transporter 1.Journal of clinical biochemistry and nutrition · 2024Article
- Time course of pulmonary inflammation and trace element biodistribution during and after sub-acute inhalation exposure to copper oxide nanoparticles in a murine model.Particle and fibre toxicology · 2022Article
- Molecular Mechanism of Nramp-Family Transition Metal Transport.Journal of molecular biology · 2021Review
- 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
- Designing yeast as plant-like hyperaccumulators for heavy metals.Nature communications · 2019Article
- Article
- S-Nitrosylation of Divalent Metal Transporter 1 Enhances Iron Uptake to Mediate Loss of Dopaminergic Neurons and Motoric Deficit.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- A Functional Study Identifying Critical Residues Involving Metal Transport Activity and Selectivity in Natural Resistance-Associated Macrophage Protein 3 inInternational journal of molecular sciences · 2018Article
- Bioinformatic and Functional Analysis of a Key Determinant Underlying the Substrate Selectivity of the Al Transporter, Nrat1.Frontiers in plant science · 2018Article
- Crystal Structure and Conformational Change Mechanism of a Bacterial Nramp-Family Divalent Metal Transporter.Structure (London, England : 1993) · 2016Article
- Conserved methionine dictates substrate preference in Nramp-family divalent metal transporters.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Divalent metal transporter 1 (DMT1) in the brain: implications for a role in iron transport at the blood-brain barrier, and neuronal and glial pathology.Frontiers in molecular neuroscience · 2015Review
- Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transport.Nature structural & molecular biology · 2014Article
- Pathophysiology of the Belgrade rat.Frontiers in pharmacology · 2014Review
- Pharmacology of iron transport.Annual review of pharmacology and toxicology · 2013Review
- Mechanisms of mammalian iron homeostasis.Biochemistry · 2012Review
- H(+)-coupled divalent metal-ion transporter-1: functional properties, physiological roles and therapeutics.Current topics in membranes · 2012Review
- Interaction of calcium with the human divalent metal-ion transporter-1.Biochemical and biophysical research communications · 2010Article
- Activating mutations of the TRPML1 channel revealed by proline-scanning mutagenesis.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Divalent metal transporter-1 (DMT1/DCT1/Nramp2) is the major Fe(2+) transporter mediating cellular iron uptake in mammals. Phenotypic analyses of animals with spontaneous mutations in DMT1 indicate that it functions at two distinct sites, transporting dietary iron across the apical membrane of intestinal absorptive cells, and transporting endosomal iron released from transferrin into the cytoplasm of erythroid precursors. DMT1 also acts as a proton-dependent transporter for other heavy metal ions including Mn(2+), Co(2+), and Cu(2), but not for Mg(2+) or Ca(2+). A unique mutation in DMT1, G185R, has occurred spontaneously on two occasions in microcytic (mk) mice and once in Belgrade (b) rats. This mutation severely impairs the iron transport capability of DMT1, leading to systemic iron deficiency and anemia. The repeated occurrence of the G185R mutation cannot readily be explained by hypermutability of the gene. Here we show that G185R mutant DMT1 exhibits a new, constitutive Ca(2+) permeability, suggesting a gain of function that contributes to remutation and the mk and b phenotypes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.