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

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

3.0K
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...
3.0K
Non-gated Ion Channels01:24

Non-gated Ion Channels

7.6K
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....
7.6K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

7.1K
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...
7.1K
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

5.0K
GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
5.0K
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

3.4K
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....
3.4K
Ion Channels01:19

Ion Channels

89.1K
The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow...
89.1K

You might also read

Related Articles

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

Sort by
Same author

Opening closed inward rectifier potassium channel doors.

British journal of pharmacology·2026
Same author

Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.

Nature communications·2025
Same author

Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.

bioRxiv : the preprint server for biology·2025
Same author

PIP2-driven cytoplasmic domain motions are coupled to Kir2 channel gating.

The Journal of general physiology·2025
Same author

The sodium/glucose cotransporter 2 inhibitor empagliflozin is a pharmacological chaperone of cardiac Na<sub>v</sub>1.5 channels.

American journal of physiology. Heart and circulatory physiology·2025
Same author

Ethosuximide: Subunit- and Gβγ-dependent blocker and reporter of allosteric changes in GIRK channels.

British journal of pharmacology·2025

Related Experiment Video

Updated: Oct 22, 2025

One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

24.8K

Simulating PIP2-Induced Gating Transitions in Kir6.2 Channels.

Michael Bründl1, Sarala Pellikan1, Anna Stary-Weinzinger1

  • 1Department of Pharmaceutical Sciences, Division of Pharmacology and Toxicology, University of Vienna, Vienna, Austria.

Frontiers in Molecular Biosciences
|August 27, 2021
PubMed
Summary

ATP-sensitive potassium (KATP) channels regulate cell metabolism. Molecular Dynamics simulations reveal how phosphatidyl-inositol 4,5-bisphosphate (PIP2) activates Kir6.2 channels, crucial for understanding channel gating and related diseases.

Keywords:
Kir6.2L164PPIP2molecular dynamics simulationspermanent neonatal diabetespore diameter

More Related Videos

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

13.7K
Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

17.6K

Related Experiment Videos

Last Updated: Oct 22, 2025

One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

24.8K
Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

13.7K
Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

17.6K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Structural Biology

Background:

  • ATP-sensitive potassium (KATP) channels, comprising Kir6.2 and SUR subunits, link cellular metabolism to K+ flux.
  • Channel dysfunction is implicated in neonatal diabetes and other diseases.
  • K+ permeation is controlled by conformational changes, with G-loop and selectivity filter potentially involved in gating.

Purpose of the Study:

  • To investigate the molecular mechanism of PIP2 activation in KATP channels.
  • To elucidate the structural basis of PIP2 binding and its role in Kir6.2 channel gating.
  • To combine molecular dynamics simulations with functional data to understand PIP2 regulation.

Main Methods:

  • Utilized Molecular Dynamics (MD) simulations to analyze the dynamics of Kir6.2 gating residues.
  • Integrated simulation data with existing functional studies on KATP channel regulation.
  • Focused on the interaction between PIP2 and the Kir6.2 subunit.

Main Results:

  • MD simulations provided insights into the dynamic behavior of Kir6.2 residues involved in gating.
  • The study explored the structural determinants of PIP2 binding, which were previously unresolved in cryo-EM structures.
  • Identified potential mechanisms for PIP2-mediated regulation of KATP channel activity.

Conclusions:

  • The findings offer a deeper understanding of PIP2's role in activating KATP channels at a molecular level.
  • This research bridges structural and functional data to explain Kir6.2 channel gating.
  • The study provides a foundation for further investigation into KATP channelopathies and therapeutic strategies.