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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
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Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Non-gated Ion Channels01:24

Non-gated Ion Channels

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Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
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The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

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A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential....
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Updated: Mar 8, 2026

Pull-down of Calmodulin-binding Proteins
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Pull-down of Calmodulin-binding Proteins

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Calmodulin limits pathogenic Na+ channel persistent current.

Haidun Yan1, Chaojian Wang1, Steven O Marx2,3

  • 1Ion Channel Research Unit, Duke University Medical Center, Durham, NC 27710.

The Journal of General Physiology
|January 15, 2017
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) binding to sodium channel C-terminal domains limits persistent current, preventing arrhythmias and epilepsy. Restoring CaM binding corrects defects in voltage-gated Na+ channels.

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Area of Science:

  • Molecular neuroscience
  • Ion channel biophysics
  • Cardiac and neurological channelopathies

Background:

  • Delayed inactivation of voltage-gated sodium (NaV) channels causes persistent Na+ current, linked to cardiac arrhythmias and epilepsy.
  • The molecular mechanisms underlying NaV channel inactivation defects remain largely unknown.

Purpose of the Study:

  • To investigate the role of calmodulin (CaM) in regulating NaV channel inactivation.
  • To identify molecular contributors to NaV channel inactivation defects and potential therapeutic targets.

Main Methods:

  • Investigated CaM binding to NaV channel intracellular C-terminal domains (CTDs).
  • Analyzed effects of disease-associated mutations on CaM binding and channel function.
  • Utilized electrophysiology and biochemical assays to assess CaM's impact on NaV channel activity.

Main Results:

  • CaM binding to NaV CTDs limits persistent Na+ current and accelerates inactivation across the NaV family.
  • Mutations causing arrhythmias (NaV1.5) or epilepsy (NaV1.2) reduce CaM binding to CTDs.
  • Increasing CaM availability restores normal inactivation in mutant channels and reduces persistent current in wild-type NaV1.6.

Conclusions:

  • CaM acts as a critical regulator of NaV channel inactivation by binding to CTDs.
  • Reduced CaM binding due to mutations contributes to channelopathies like arrhythmias and epilepsy.
  • Modulating CaM availability may offer a therapeutic strategy for treating NaV channel-related disorders.