ArticleThe Journal of general physiology2008
Molecular template for a voltage sensor in a novel K+ channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel.
Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Modular architecture of KEMBO reports · 2025Review
- Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020Review
- Extended beta distributions open the access to fast gating in bilayer experiments-assigning the voltage-dependent gating to the selectivity filter.FEBS letters · 2017Article
- A new mechanism of voltage-dependent gating exposed by KThe Journal of general physiology · 2017Article
- hERG S4-S5 linker acts as a voltage-dependent ligand that binds to the activation gate and locks it in a closed state.Scientific reports · 2017Article
- Isolated pores dissected from human two-pore channel 2 are functional.Scientific reports · 2016Article
- The Sensorless Pore Module of Voltage-gated K+ Channel Family 7 Embodies the Target Site for the Anticonvulsant Retigabine.The Journal of biological chemistry · 2016Article
- Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Biophysical journal · 2016Review
- Lipid bilayer modules as determinants of K+ channel gating.The Journal of biological chemistry · 2014Article
- PIP2 regulation of KCNQ channels: biophysical and molecular mechanisms for lipid modulation of voltage-dependent gating.Frontiers in physiology · 2014Review
- Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Neuron · 2013Review
- Potassium ion channels: could they have evolved from viruses?Plant physiology · 2013Review
- Stabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanism.The Journal of biological chemistry · 2013Article
- The voltage-sensing domain of a phosphatase gates the pore of a potassium channel.The Journal of general physiology · 2013Article
- Article
- Crystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes.The Journal of biological chemistry · 2012Article
- Perspectives on: conformational coupling in ion channels: thermodynamics of electromechanical coupling in voltage-gated ion channels.The Journal of general physiology · 2012Article
- Tetrameric assembly of KvLm K+ channels with defined numbers of voltage sensors.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
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3 authors.
Funding
Abstract
KvLm is a prokaryotic voltage-gated K(+) (Kv) channel from Listeria monocytogenes. The sequence of the voltage-sensing module (transmembrane segments S1-S4) of KvLm is atypical in that it contains only three of the eight conserved charged residues known to be deterministic for voltage sensing in eukaryotic Kv's. In contrast, the pore module (PM), including the S4-S5 linker and cytoplasmic tail (linker-S5-P-S6-C-terminus) of KvLm, is highly conserved. Here, the full-length (FL)-KvLm and the KvLm-PM only proteins were expressed, purified, and reconstituted into giant liposomes. The properties of the reconstituted FL-KvLm mirror well the characteristics of the heterologously expressed channel in Escherichia coli spheroplasts: a right-shifted voltage of activation, micromolar tetrabutylammonium-blocking affinity, and a single-channel conductance comparable to that of eukaryotic Kv's. Conversely, ionic currents through the PM recapitulate both the conductance and blocking properties of the FL-KvLm, yet the KvLm-PM exhibits only rudimentary voltage dependence. Given that the KvLm-PM displays many of the conduction properties of FL-KvLm and of other eukaryotic Kv's, including strict ion selectivity, we conclude that self-assembly of the PM subunits in lipid bilayers, in the absence of the voltage-sensing module, generates a conductive oligomer akin to that of the native KvLm, and that the structural independence of voltage sensing and PMs observed in eukaryotic Kv channels was initially implemented by nature in the design of prokaryotic Kv channels. Collectively, the results indicate that this robust functional module will prove valuable as a molecular template for coupling new sensors and to elucidate PM residue-specific contributions to Kv conduction properties.
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