Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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...
Regulation of Sodium and Potassium01:26

Regulation of Sodium and Potassium

The regulation of sodium and potassium ion concentrations in the human body is a complex process governed primarily by hormones such as aldosterone, antidiuretic hormone (ADH), and atrial natriuretic peptide (ANP).
Sodium Regulation
Sodium ions make up approximately 90% of extracellular cations, with a normal blood plasma concentration of 136–148 mEq/L. A decrease in blood volume and pressure triggers the release of renin from granular cells in the juxtaglomerular complex (JGC), primarily in...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

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.
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Extracellular K<sup>+</sup> modulates the pore conformations of Cys-loop receptor anion channels.

Nature communications·2026
Same author

Ca<sup>2+</sup> influx through muscle-type nicotinic acetylcholine receptors in zebrafish contributes to contractions and development of slow muscle cells in early development.

Open biology·2025
Same author

Compound heterozygous variants of CACNA1H change channel properties and contribute to intractable epilepsy with myoclonic-atonic seizures.

Journal of human genetics·2025
Same author

Extracellular salt bridge networks around S4 implicated in HCN channel gating and heart disease.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Characterization and Engineering of a Blue-Sensitive, Gi/o-Biased, and Bistable Ciliary Opsin from a Fan Worm.

Biochemistry·2025
Same author

Identification of KCNE6, a new member of the KCNE family of potassium channel auxiliary subunits.

Communications biology·2024

Related Experiment Video

Updated: Jun 1, 2026

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

Nano-environmental changes by KCNE proteins modify KCNQ channel function.

Koichi Nakajo1, Yoshihiro Kubo

  • 1National Institute for Physiological Sciences, Okazaki, Japan. knakajo@nips.ac.jp

Channels (Austin, Tex.)
|June 10, 2011
PubMed
Summary

The KCNQ1 channel

Area of Science:

  • Molecular biology
  • Ion channel physiology
  • Biophysics

Background:

  • KCNQ1 is a voltage-dependent potassium channel crucial in various human tissues.
  • KCNE proteins act as auxiliary subunits, significantly altering KCNQ1 channel function.
  • The precise mechanisms of KCNQ1 regulation by KCNE proteins remain incompletely understood.

Purpose of the Study:

  • To review recent findings on KCNQ1 channel regulation by KCNE proteins.
  • To explore the roles of different KCNQ1 channel domains in KCNE protein interaction.
  • To discuss the flexible stoichiometry of KCNQ1-KCNE1 complexes.

Main Methods:

  • Literature review of recent studies on KCNQ1-KCNE protein interactions.
  • Analysis of experimental data concerning KCNQ1 channel domains (pore and voltage-sensing).

More Related Videos

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
10:59

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Published on: February 10, 2014

Related Experiment Videos

Last Updated: Jun 1, 2026

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors
10:59

Use of Label-free Optical Biosensors to Detect Modulation of Potassium Channels by G-protein Coupled Receptors

Published on: February 10, 2014

  • Examination of KCNQ1-KCNE1 complex stoichiometry.

    • Main Results:

    • Evidence suggests both pore and voltage-sensing domains of KCNQ1 are involved in KCNE protein regulation.
    • The stoichiometry of KCNQ1-KCNE1 complexes is flexible, not fixed.
    • KCNQ1 channels can associate with up to four KCNE1 proteins.

    Conclusions:

    • KCNE protein regulation of KCNQ1 channels involves complex interactions across multiple channel domains.
    • Flexible stoichiometry in KCNQ1-KCNE1 complexes adds another layer to channel regulation.
    • Further research is needed to fully elucidate these intricate regulatory mechanisms.