ArticleScientific reports2016
Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Biosynthesis and function of magnetic organelles in magnetotactic bacteria.Nature reviews. Microbiology · 2026Review
- MamF-like proteins are distant Tic20 homologs involved in organelle assembly in bacteria.Nature communications · 2024Article
- Comparing the Colloidal Stabilities of Commercial and Biogenic Iron Oxide Nanoparticles That Have Potential In Vitro/In Vivo Applications.Molecules (Basel, Switzerland) · 2023Article
- Treatable Hereditary Manganese Transport Disorder: NovelJournal of pediatric genetics · 2021Article
- Metal transport mechanism of the cation diffusion facilitator (CDF) protein family - a structural perspective on human CDF (ZnT)-related diseases.RSC chemical biology · 2021Review
- 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
- Why and how to investigate the role of protein phosphorylation in ZIP and ZnT zinc transporter activity and regulation.Cellular and molecular life sciences : CMLS · 2020Review
- Article
- The Potential of Intrinsically Magnetic Mesenchymal Stem Cells for Tissue Engineering.International journal of molecular sciences · 2018Review
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10 authors.
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Abstract
Cation diffusion facilitators (CDF) are highly conserved, metal ion efflux transporters that maintain divalent transition metal cation homeostasis. Most CDF proteins contain two domains, the cation transporting transmembrane domain and the regulatory cytoplasmic C-terminal domain (CTD). MamM is a magnetosome-associated CDF protein essential for the biomineralization of magnetic iron-oxide particles in magnetotactic bacteria. To investigate the structure-function relationship of CDF cytoplasmic domains, we characterized a MamM M250P mutation that is synonymous with the disease-related mutation L349P of the human CDF protein ZnT-10. Our results show that the M250P exchange in MamM causes severe structural changes in its CTD resulting in abnormal reduced function. Our in vivo, in vitro and in silico studies indicate that the CTD fold is critical for CDF proteins' proper function and support the previously suggested role of the CDF cytoplasmic domain as a CDF regulatory element. Based on our results, we also suggest a mechanism for the effects of the ZnT-10 L349P mutation in human.
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