Related Experiment Video
Updated: Jun 5, 2025

Isolating and Culturing Vestibular and Spiral Ganglion Somata from Neonatal Rodents for Patch-Clamp Recordings
Published on: April 21, 2023
Multiple gating processes associated with the distal end of the S6 segment of domain II in the Nav channels
Minzhi Chen1, Shuijiao Peng2, Zhen Xiao1
1The National and Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, China; Peptide and Small Molecule Drug R&D Platform, Furong Laboratory, Hunan Normal University, Changsha, Hunan, China; Institute of Interdisciplinary Studies, Hunan Normal University, Changsha, China.
Abstract:
Voltage-gated sodium (Nav) channels are transmembrane proteins that play crucial roles in the initiation and propagation of action potentials (APs) in excitable tissues such as the heart, muscles, and nerves. The distal ends of the four domain S6 segments of Nav channels contain hydrophobic residues, which form an intracellular gate. This gate allows Nav channels to control ion flux in excitable cells by opening and closing. However, the mechanism of the distal end of Domain II (DII) S6 segment in channel gating remains unclear. In this study, using whole-cell patch clamp recording, we systematically investigated the biophysical characteristics of various mutants L811 site (located at the distal end of the DII S6 segment) of Nav1.9 and the corresponding L796P mutant of Nav1.4. We found that the mutations significantly shifted the activation and inactivation curves, slowed the fast inactivation, accelerated the slow inactivation and use-dependent slow inactivation, and L811P altered the ion selectivity of the channel. Therefore, our findings suggest that the distal end of the DII S6 segment in Nav channels plays a pivotal role in regulating multiple gating processes.
More Related Videos
11:42Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
Published on: January 22, 2015
12:26Author Spotlight: Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
Published on: June 2, 2023
Related Concept Videos
Ligand-Gated Ion Channel Receptor: Gating Mechanism
Voltage-gated Ion Channels
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...
Non-gated Ion Channels
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism....
Mechanically-gated Ion Channels
The Role of Ion Channels in Neuronal Computation
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....
Ligand-gated Ion Channels
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...