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Two-sided block of a dual-topology F − channel
Abstract
Significance: The study's significance is in its novelty along several lines. First, the ion channel studied, a Fluc F − channel, is recently discovered and has been only sparsely studied yet; this work adds a piece of the puzzle to the channel's mechanistic landscape. Second, this is the first channel, to our knowledge, for which two-sided blocking has been observed; this type of blocking is a consequence of the unusual dual-topology assembly of Fluc channels. Third, the mathematical analysis of this kind of block is novel (necessarily so). Fourth, the main result—that the two ends of the pore can be simultaneously occupied by blockers but with negative cooperativity in binding—provokes future structural and mechanistic experiments.
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Proteins encoded by the crcB genes are electrodiffusive F− channels.
“Electrophysiological characterization showed that the proteins encoded by the crcB genes are electrodiffusive F− channels (2, 3, 60–63), and they were renamed Fluc (Fluoride channel) in bacteria and FEX (Fluoride exporter) in eukaryotes.”
From Membrane exporters of fluoride ion (2021) · cites this paper as [61]
Single Fluc channels can be monitored in planar lipid bilayer electrophysiological recordings, where fluoride conductances correspond to a throughput of ~10^5-6 ions/sec.
“In harmony with an electrodiffusive mechanism, single Fluc channels can be monitored in planar lipid bilayer electrophysiological recordings, where the fluoride conductances observed correspond to a throughput of ~105–6 ions/sec(2, 61).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [61]
An inhibitor applied in sequence to the cis and trans sides of a single Fluc channel in a planar lipid bilayer blocks both sides of the channel with identical kinetics.
“Functional experiments support this observation: an inhibitor applied in sequence to the cis and trans sides of a single Fluc channel in a planar lipid bilayer blocks both sides of the channel with identical kinetics (60–62).”
From Membrane exporters of fluoride ion (2021) · cites this paper as [61]
For F85I and F82I, efflux of F- is 2 and 3 orders of magnitude slower, respectively, than for wild type (~3x10^5 s-1).
“For F85I and F82I, efflux of F- is 2 and 3 orders of magnitude slower, respectively, than for wild type (~3x105 s-1)15”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [15]
The paucity of salt-bridges rationalizes the rather weak ionic strength dependence of monobody binding.
“the paucity of salt-bridges rationalizing the rather weak ionic strength dependence of monobody binding15.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [15]
The structures represent the monobody-blocked state similar to that observed electrophysiologically.
“The structures here would represent the monobody-blocked state similar to that observed electrophysiologically6,15.”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [15]
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Research works printed but not linked: 6
- 10.1126/science.1215063 · DOI · Paper page
- 10.1038/ncomms6120 · DOI · Paper page
- RB Stockbridge, JL Robertson, L Kolmakova-Partensky, C Miller, A family of fluoride-specific ion channels with dual-topology architecture. eLife 2, e01084 (2013). · DOI · Paper page
- 10.1016/B978-0-12-396962-0.00006-9 · DOI · Paper page
- 10.1085/jgp.91.3.317 · DOI
- 10.1085/jgp.201110684 · DOI
Cited by
Sorted by citations
Crystal structures of a double-barrelled fluoride ion channel
Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119
Self-citationMembrane exporters of fluoride ion
McIlwain, B. C., Ruprecht, M. T., & Stockbridge, R. B. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-071520-112507 · Cited by 69
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Metadata
- Authors
- Turman, D. L., Nathanson, J. T., Stockbridge, R. B., Street, T. O., & Miller, C.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2015-04-20
- Volume
- 112
- Issue
- 18
- Pages
- 5697-5701
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 22
- References
- 0
- Language
- en
- Funders
- HHS | NIH | National Institute of General Medical Sciences (RO1-GM107023)
- Howard Hughes Medical Institute (none)
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