ArticleProceedings of the National Academy of Sciences of the United States of America2002
An exchanger-like protein underlies the large Mg2+ current in Paramecium.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Micromanipulation in Paramecium: From non-mendelian inheritance to the outlook for versatile micromachines.The Journal of eukaryotic microbiology · 2022Review
- Review
- UsingGenes · 2021Review
- A Novel Role for Polycystin-2 (Pkd2) inGenes · 2019Article
- Review
- Proteomic analysis of the cilia membrane of Paramecium tetraurelia.Journal of proteomics · 2013Article
- Protein Phylogenetic Analysis of Ca(2+)/cation Antiporters and Insights into their Evolution in Plants.Frontiers in plant science · 2012Article
- Ion channels in microbes.Physiological reviews · 2008Review
- Effects of intracellular and extracellular concentrations of Ca2+, K+, and Cl- on the Na+-dependent Mg2+ efflux in rat ventricular myocytes.Biophysical journal · 2006Article
- Transport of magnesium and other divalent cations: evolution of the 2-TM-GxN proteins in the MIT superfamily.Molecular genetics and genomics : MGG · 2005Article
- Article
- PAK paradox: Paramecium appears to have more K(+)-channel genes than humans.Eukaryotic cell · 2003Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
There are very few molecules known to transport Mg(2+) in eukaryotes. The membrane of Paramecium tetraurelia passes a large Mg(2+)-selective current and exhibits a corresponding backward swimming behavior. Both are missing in a group of mutants called eccentric. By sorting an indexed WT genomic library through microinjection into the macronucleus, we have isolated a DNA fragment that complements the eccentric mutations. The Mg(2+) currents and behavior are restored fully in the transformed cells. Surprisingly, the conceptually translated protein is not homologous to any known ion channel but instead has some similarity to K(+)-dependent Na(+)Ca(2+) exchangers. Exchangers are either electrically silent or only pass very small and slow currents compared with ion-channel currents. In light of recent ion-channel crystal structures and considering the need to have narrow ion-selective filters, we speculate on how an exchanger might evolve to show channel-like activities in special circumstances. The significance of finding the molecular basis of a Mg(2+)-specific pathway is also discussed.
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Registered trials
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