ArticleThe Journal of physiology2005
Modulation of skeletal and cardiac voltage-gated sodium channels by calmodulin.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.
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Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.
- Variability in reported midpoints of (in)activation of cardiac INa.The Journal of general physiology · 2025Pooled it
- Nernst-Planck-Gaussian finite element modelling of CaFrontiers in physiology · 2024Article
- NaStructure (London, England : 1993) · 2021Article
- Ca2+-dependent modulation of voltage-gated myocyte sodium channels.Biochemical Society transactions · 2021Review
- Electrophysiological and Proarrhythmic Effects of Hydroxychloroquine Challenge in Guinea-Pig Hearts.ACS pharmacology & translational science · 2021Article
- Finite element analysis predicts CaScientific reports · 2021Article
- Review
- Sarcoplasmic reticular CaScientific reports · 2021Article
- Small G-protein RhoA is a potential inhibitor of cardiac fast sodium current.Journal of physiology and biochemistry · 2021Article
- Improved sequence-based prediction of interaction sites in α-helical transmembrane proteins by deep learning.Computational and structural biotechnology journal · 2021Article
- Role of the disulfide bond on the structure and activity of μ-conotoxin PIIIA in the inhibition of NaRSC advances · 2019Article
- Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaBiomolecular NMR assignments · 2018Article
- A Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.Structure (London, England : 1993) · 2018Article
- Voltage-Gated Sodium Channel β1/β1B Subunits Regulate Cardiac Physiology and Pathophysiology.Frontiers in physiology · 2018Review
- Voltage-dependent inward currents in smooth muscle cells of skeletal muscle arterioles.PloS one · 2018Article
- Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaBiophysical chemistry · 2017Article
- Murine Electrophysiological Models of Cardiac Arrhythmogenesis.Physiological reviews · 2017Review
- Intracellular calcium attenuates late current conducted by mutant human cardiac sodium channels.Circulation. Arrhythmia and electrophysiology · 2015Article
- Physiological and Pathophysiological Insights of Nav1.4 and Nav1.5 Comparison.Frontiers in pharmacology · 2015Review
- Post-translational modifications of voltage-gated sodium channels in chronic pain syndromes.Frontiers in pharmacology · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Calmodulin (CaM) has been shown to modulate different ion channels, including voltage-gated sodium channels (NaChs). Using the yeast two-hybrid assay, we found an interaction between CaM and the C-terminal domains of adult skeletal (NaV1.4) and cardiac (NaV1.5) muscle NaChs. Effects of CaM were studied using sodium channels transiently expressed in CHO cells. Wild type CaM (CaM(WT)) caused a hyperpolarizing shift in the voltage dependence of activation and inactivation for NaV1.4 and activation for NaV1.5. Intracellular application of CaM caused hyperpolarizing shifts equivalent to those seen with CaM(WT) coexpression with NaV1.4. Elevated Ca2+ and CaM-binding peptides caused depolarizing shifts in the inactivation curves seen with CaM(WT) coexpression with NaV1.4. KN93, a CaM-kinase II inhibitor, had no effect on NaV1.4, suggesting that CaM acts directly on NaV1.4 and not through activation of CaM-kinase II. Coexpression of hemi-mutant CaMs showed that an intact N-terminal lobe of CaM is required for effects of CaM upon NaV1.4. Mutations in the sodium channel IQ domain disrupted the effects of CaM on NaV1.4: the I1727E mutation completely blocked all calmodulin effects, while the L1736R mutation disrupted the effects of Ca2+-calmodulin on inactivation. Chimeric channels of NaV1.4 and NaV1.5 also indicated that the C-terminal domain is largely responsible for CaM effects on inactivation. CaM had little effect on NaV1.4 expressed in HEK cells, possibly due to large differences in the endogenous expression of beta-subunits between CHO and HEK cells. These results in heterologous cells suggest that Ca2+ released during muscle contraction rapidly modulates NaCh availability via CaM.
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