ArticleBiophysical journal2007
Acidic residues on the voltage-sensor domain determine the activation of the NaChBac sodium channel.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- In vitro discovery of novel prokaryotic ion channel candidates for antiarrhythmic gene therapy.Methods in enzymology · 2021Article
- Isoflurane modulates activation and inactivation gating of the prokaryotic NaThe Journal of general physiology · 2017Article
- Engineering prokaryotic channels for control of mammalian tissue excitability.Nature communications · 2016Article
- Charged Residues at the First Transmembrane Region Contribute to the Voltage Dependence of the Slow Gate of Connexins.The Journal of biological chemistry · 2016Article
- Modulation of a voltage-gated Na+ channel by sevoflurane involves multiple sites and distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Investigating the size and dynamics of voltage-gated sodium channel fenestrations.Channels (Austin, Tex.) · 2014Article
- A gating charge interaction required for late slow inactivation of the bacterial sodium channel NavAb.The Journal of general physiology · 2013Article
- Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel.Biochimica et biophysica acta · 2012Article
- Local anesthetic inhibition of a bacterial sodium channel.The Journal of general physiology · 2012Article
- NaChBac: the long lost sodium channel ancestor.Biochemistry · 2011Article
- Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels.The Journal of biological chemistry · 2011Article
- Y1767C, a novel SCN5A mutation, induces a persistent Na+ current and potentiates ranolazine inhibition of Nav1.5 channels.American journal of physiology. Heart and circulatory physiology · 2011Article
- Coupling between residues on S4 and S1 defines the voltage-sensor resting conformation in NaChBac.Biophysical journal · 2010Article
- An aqueous H+ permeation pathway in the voltage-gated proton channel Hv1.Nature structural & molecular biology · 2010Article
- Studies of alpha-helicity and intersegmental interactions in voltage-gated Na+ channels: S2D4.PloS one · 2009Article
- Nardilysin convertase regulates the function of the maxi-K channel isoform mK44 in human myometrium.American journal of physiology. Cell physiology · 2009Article
- Ion channels in microbes.Physiological reviews · 2008Review
- Models of voltage-dependent conformational changes in NaChBac channels.Biophysical journal · 2008Article
- Disulfide locking a sodium channel voltage sensor reveals ion pair formation during activation.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-sensing domain of voltage-gated ion channels is characterized by specific, conserved, charged residues. Positively charged residues on segment S4 are the main contributors to voltage-sensing and negatively charged residues on the S2 and S3 segments are believed to participate to the process. However, their function in the voltage sensor is not well understood. To probe the role of three acidic residues in NaChBac (D-58 and E-68 in S2, and D-91 in S3), we employed site-directed mutagenesis to substitute native acidic residues with cysteine (neutral), lysine (positive charge), or either aspartate or glutamate (negative charge). We used a combination of the patch-clamp technique to record Na+ currents and molecular modeling to visualize interacting amino acid residues. We suggest that the acidic residues on the S2 and S3 segments form specific interactions with adjacent amino acids in the voltage-sensor domain. The main interactions in NaChBac are D-58 (S2) with A-97-G-98 (S3) and R-120 (S4), E-68 (S2) with R-129 (L4-5), and D-91 (S3) with R-72 (S2). Changing these acidic residues modified the interactions, which in turn altered the sensitivity of the voltage sensor.
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