ArticleThe Journal of biological chemistry2012
Ferritin protein nanocage ion channels: gating by N-terminal extensions.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 71 citations in OpenAlex.
- A deep dive into ferritin nanoparticle advancements: experimental and computational perspectives.Discover nano · 2026Review
- Ferroptosis: iron release mechanisms in the bioenergetic process.Cancer metastasis reviews · 2025Review
- Biocomposite Polyvinyl Alcohol/Ferritin Hydrogels with Enhanced Stretchability and Conductivity for Flexible Strain Sensors.Gels (Basel, Switzerland) · 2025Article
- Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Nanoformulation of the Broad-Spectrum Hydrophobic Antiviral Vacuolar ATPase Inhibitor Diphyllin in Human RecombinantInternational journal of nanomedicine · 2024Article
- A novel view of ferritin in cancer.Biochimica et biophysica acta. Reviews on cancer · 2023Review
- Ferritin: A Promising Nanoreactor and Nanocarrier for Bionanotechnology.ACS bio & med chem Au · 2022Review
- Structural characterization of the Myxococcus xanthus encapsulin and ferritin-like cargo system gives insight into its iron storage mechanism.Structure (London, England : 1993) · 2022Article
- Crystallographic characterization of a marine invertebrate ferritin from the sea cucumber Apostichopus japonicus.FEBS open bio · 2022Article
- Ferritin - from iron, through inflammation and autoimmunity, to COVID-19.Journal of autoimmunity · 2022Review
- Ferroptosis: Redox Imbalance and Hematological Tumorigenesis.Frontiers in oncology · 2022Review
- Dps-DNA interaction in Marinobacter hydrocarbonoclasticus protein: effect of a single-charge alteration.European biophysics journal : EBJ · 2021Article
- Flavin-mediated reductive iron mobilization from frog M and Mycobacterial ferritins: impact of their size, charge and reactivities with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.FEBS open bio · 2021Article
- Tissue Specific Fate of Nanomaterials by Advanced Analytical Imaging Techniques - A Review.Chemical research in toxicology · 2020Review
- Designability of Aromatic Interaction Networks atMolecules (Basel, Switzerland) · 2017Article
- From Dose to Response: In Vivo Nanoparticle Processing and Potential Toxicity.Advances in experimental medicine and biology · 2017Review
- L-Ferritin targets breast cancer stem cells and delivers therapeutic and imaging agents.Oncotarget · 2016Article
- Fe(2+) substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- Time-lapse anomalous X-ray diffraction shows how Fe(2+) substrate ions move through ferritin protein nanocages to oxidoreductase sites.Acta crystallographica. Section D, Biological crystallography · 2015Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Ferritin protein nanocages, self-assembled from four-α-helix bundle subunits, use Fe(2+) and oxygen to synthesize encapsulated, ferric oxide minerals. Ferritin minerals are iron concentrates stored for cell growth. Ferritins are also antioxidants, scavenging Fenton chemistry reactants. Channels for iron entry and exit consist of helical hairpin segments surrounding the 3-fold symmetry axes of the ferritin nanocages. We now report structural differences caused by amino acid substitutions in the Fe(2+) ion entry and exit channels and at the cytoplasmic pores, from high resolution (1.3-1.8 Å) protein crystal structures of the eukaryotic model ferritin, frog M. Mutations that eliminate conserved ionic or hydrophobic interactions between Arg-72 and Asp-122 and between Leu-110 and Leu-134 increase flexibility in the ion channels, cytoplasmic pores, and/or the N-terminal extensions of the helix bundles. Decreased ion binding in the channels and changes in ordered water are also observed. Protein structural changes coincide with increased Fe(2+) exit from dissolved, ferric minerals inside ferritin protein cages; Fe(2+) exit from ferritin cages depends on a complex, surface-limited process to reduce and dissolve the ferric mineral. High concentrations of bovine serum albumin or lysozyme (protein crowders) to mimic the cytoplasm restored Fe(2+) exit in the variants to wild type. The data suggest that fluctuations in pore structure control gating. The newly identified role of the ferritin subunit N-terminal extensions in gating Fe(2+) exit from the cytoplasmic pores strengthens the structural and functional analogies between ferritin ion channels in the water-soluble protein assembly and membrane protein ion channels gated by cytoplasmic N-terminal peptides.
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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.