ArticlePloS one2014
Cation diffusion facilitators transport initiation and regulation is mediated by cation induced conformational changes of the cytoplasmic domain.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Biosynthesis and function of magnetic organelles in magnetotactic bacteria.Nature reviews. Microbiology · 2026Review
- Structural and functional insights of ZnT1 C-terminal domain as a regulator of zinc transport.Scientific reports · 2025Article
- Therapeutic Innovations in Nanomedicine: Exploring the Potential of Magnetotactic Bacteria and Bacterial Magnetosomes.International journal of nanomedicine · 2025Review
- Flipping the switch: dynamic modulation of membrane transporter activity in bacteria.Microbiology (Reading, England) · 2023Review
- Energy coupling and stoichiometry of ZneLife · 2023Article
- Structural Insights into the Dimeric Form ofBiomolecules · 2022Article
- Metalloprotein-Specific or Critical Amino Acid Residues: Perspectives on Plant-Precise Detoxification and Recognition Mechanisms under Cadmium Stress.International journal of molecular sciences · 2022Review
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Metal transport mechanism of the cation diffusion facilitator (CDF) protein family - a structural perspective on human CDF (ZnT)-related diseases.RSC chemical biology · 2021Review
- Zinc: Multidimensional Effects on Living Organisms.Biomedicines · 2021Review
- Heterologous Expression and Biochemical Characterization of the Human Zinc Transporter 1 (ZnT1) and Its Soluble C-Terminal Domain.Frontiers in chemistry · 2021Article
- The cation diffusion facilitator protein MamM's cytoplasmic domain exhibits metal-type dependent binding modes and discriminates against MnThe Journal of biological chemistry · 2020Article
- The metal binding site composition of the cation diffusion facilitator protein MamM cytoplasmic domain impacts its metal responsivity.Scientific reports · 2020Article
- From conservation to structure, studies of magnetosome associated cation diffusion facilitators (CDF) proteins in Proteobacteria.PloS one · 2020Article
- The Cation Diffusion Facilitator Family Protein EmfA Confers Resistance to Manganese Toxicity in Brucella abortus 2308 and Is an Essential Virulence Determinant in Mice.Journal of bacteriology · 2019Article
- A structural overview of the zinc transporters in the cation diffusion facilitator family.Acta crystallographica. Section D, Structural biology · 2019Review
- Function, Structure, and Transport Aspects of ZIP and ZnT Zinc Transporters in Immune Cells.Journal of immunology research · 2018Review
- Physiological roles of zinc transporters: molecular and genetic importance in zinc homeostasis.The journal of physiological sciences : JPS · 2017Review
- Magnetosome biogenesis in magnetotactic bacteria.Nature reviews. Microbiology · 2016Review
- A mutagenic study identifying critical residues for the structure and function of rice manganese transporter OsMTP8.1.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cation diffusion facilitators (CDF) are part of a highly conserved protein family that maintains cellular divalent cation homeostasis in all domains of life. CDF's were shown to be involved in several human diseases, such as Type-II diabetes and neurodegenerative diseases. In this work, we employed a multi-disciplinary approach to study the activation mechanism of the CDF protein family. For this we used MamM, one of the main ion transporters of magnetosomes--bacterial organelles that enable magnetotactic bacteria to orientate along geomagnetic fields. Our results reveal that the cytosolic domain of MamM forms a stable dimer that undergoes distinct conformational changes upon divalent cation binding. MamM conformational change is associated with three metal binding sites that were identified and characterized. Altogether, our results provide a novel auto-regulation mode of action model in which the cytosolic domain's conformational changes upon ligand binding allows the priming of the CDF into its transport mode.
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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.