ArticleThe Journal of biological chemistry2011
Simplified bacterial "pore" channel provides insight into the assembly, stability, and structure of sodium channels.
Article in The Journal of biological chemistry, 2011. 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, 33 citations in OpenAlex.
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.Nature structural & molecular biology · 2022Article
- The T1-tetramerisation domain of Kv1.2 rescues expression and preserves function of a truncated NaChBac sodium channel.FEBS letters · 2022Article
- A new mechanism of voltage-dependent gating exposed by KThe Journal of general physiology · 2017Article
- Isolated pores dissected from human two-pore channel 2 are functional.Scientific reports · 2016Article
- Structure of the C-terminal domain of the prokaryotic sodium channel orthologue NsvBa.European biophysics journal : EBJ · 2016Article
- Molecular basis of ion permeability in a voltage-gated sodium channel.The EMBO journal · 2016Article
- Cell-free expression of a functional pore-only sodium channel.Protein expression and purification · 2015Article
- Bacterial voltage-gated sodium channels (BacNa(V)s) from the soil, sea, and salt lakes enlighten molecular mechanisms of electrical signaling and pharmacology in the brain and heart.Journal of molecular biology · 2015Review
- Characterization of the Prokaryotic Sodium Channel NavSp Pore with a Microfluidic Bilayer Platform.PloS one · 2015Article
- Structural model of the open-closed-inactivated cycle of prokaryotic voltage-gated sodium channels.The Journal of general physiology · 2015Review
- Selectivity filters and cysteine-rich extracellular loops in voltage-gated sodium, calcium, and NALCN channels.Frontiers in physiology · 2015Review
- Locating the route of entry and binding sites of benzocaine and phenytoin in a bacterial voltage gated sodium channel.PLoS computational biology · 2014Article
- Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels.Journal of molecular biology · 2014Article
- Investigating the size and dynamics of voltage-gated sodium channel fenestrations.Channels (Austin, Tex.) · 2014Article
- Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Neuron · 2013Review
- Domain organization of the ATP-sensitive potassium channel complex examined by fluorescence resonance energy transfer.The Journal of biological chemistry · 2013Article
- Role of the C-terminal domain in the structure and function of tetrameric sodium channels.Nature communications · 2013Article
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- Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.Nature communications · 2012Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Eukaryotic sodium channels are important membrane proteins involved in ion permeation, homeostasis, and electrical signaling. They are long, multidomain proteins that do not express well in heterologous systems, and hence, structure/function and biochemical studies on purified sodium channel proteins have been limited. Bacteria produce smaller, homologous tetrameric single domain channels specific for the conductance of sodium ions. They consist of N-terminal voltage sensor and C-terminal pore subdomains. We designed a functional pore-only channel consisting of the final two transmembrane helices, the intervening P-region, and the C-terminal extramembranous region of the sodium channel from the marine bacterium Silicibacter pomeroyi. This sodium "pore" channel forms a tetrameric, folded structure that is capable of supporting sodium flux in phospholipid vesicles. The pore-only channel is more thermally stable than its full-length counterpart, suggesting that the voltage sensor subdomain may destabilize the full-length channel. The pore subdomains can assemble, fold, and function independently from the voltage sensor and exhibit similar ligand-blocking characteristics as the intact channel. The availability of this simple pore-only construct should enable high-level expression for the testing of potential new ligands and enhance our understanding of the structural features that govern sodium selectivity and permeability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.