ArticleScientific reports2013
Structural basis for the modulation of the neuronal voltage-gated sodium channel NaV1.6 by calmodulin.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Novel NaGlia · 2026Article
- Direct binding of calmodulin to the cytosolic C-terminal regions of sweet/umami taste receptors.Journal of biochemistry · 2023Article
- Role of the voltage‑gated sodium channel Nav1.6 in glioma and candidate drugs screening.International journal of molecular medicine · 2023Article
- NaV1.6 dysregulation within myocardial T-tubules by D96V calmodulin enhances proarrhythmic sodium and calcium mishandling.The Journal of clinical investigation · 2023Article
- NaStructure (London, England : 1993) · 2021Article
- Calmodulin Interactions with Voltage-Gated Sodium Channels.International journal of molecular sciences · 2021Review
- Review
- Structural basis of cytoplasmic NaV1.5 and NaV1.4 regulation.The Journal of general physiology · 2021Review
- Article
- CaeLife · 2020Article
- Neurogranin stimulates Ca2+/calmodulin-dependent kinase II by suppressing calcineurin activity at specific calcium spike frequencies.PLoS computational biology · 2020Article
- Distinct functional alterations in SCN8A epilepsy mutant channels.The Journal of physiology · 2020Article
- CaBiochemistry · 2019Article
- Molecular Dynamics Study of the Changes in Conformation of Calmodulin with Calcium Binding and/or Target Recognition.Scientific reports · 2019Article
- Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaBiomolecular NMR assignments · 2018Article
- Environmental Enrichment and Social Isolation Mediate Neuroplasticity of Medium Spiny Neurons through the GSK3 Pathway.Cell reports · 2018Article
- Effect of Ca2+ on the promiscuous target-protein binding of calmodulin.PLoS computational biology · 2018Article
- Direct visualization of interaction between calmodulin and connexin45.The Biochemical journal · 2017Article
- Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaBiomolecular NMR assignments · 2017Article
- Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaBiophysical chemistry · 2017Article
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5 authors.
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Abstract
The neuronal-voltage gated sodium channel (VGSC), Na(V)1.6, plays an important role in propagating action potentials along myelinated axons. Calmodulin (CaM) is known to modulate the inactivation kinetics of Na(V)1.6 by interacting with its IQ motif. Here we report the crystal structure of apo-CaM:Na(V)1.6IQ motif, along with functional studies. The IQ motif of Na(V)1.6 adopts an α-helical conformation in its interaction with the C-lobe of CaM. CaM uses different residues to interact with Na(V)1.6IQ motif depending on the presence or absence of Ca²⁺. Three residues from Na(V)1.6, Arg1902, Tyr1904 and Arg1905 were identified as the key common interacting residues in both the presence and absence of Ca²⁺. Substitution of Arg1902 and Tyr1904 with alanine showed a reduced rate of Na(V)1.6 inactivation in electrophysiological experiments in vivo. Compared with other CaM:Na(V) complexes, our results reveal a different mode of interaction for CaM:Na(V)1.6 and provides structural insight into the isoform-specific modulation of VGSCs.
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