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

ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
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...
Mechanism of Ciliary Motion01:05

Mechanism of Ciliary Motion

The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
Mechanism of Ciliary Motion01:05

Mechanism of Ciliary Motion

The ciliary structures were first seen in 1647 by Antonie Leeuwenhoek while observing the protozoans. In lower organisms, these appendages are responsible for cell movement, while in higher organisms, these appendages help in the movement of the extracellular fluids within the body cavities.
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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...
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

Structural insights into GTP-coupled conformational changes in Mfn1 revealed by time-resolved transition metal ion FRET.

bioRxiv : the preprint server for biology·2025
Same author

Discovery of novel cyclopentane carboxylic acids as potent and selective inhibitors of Na<sub>V</sub>1.7.

Bioorganic & medicinal chemistry letters·2024
Same author

Molecular Pharmacology of Selective Na<sub>V</sub>1.6 and Dual Na<sub>V</sub>1.6/Na<sub>V</sub>1.2 Channel Inhibitors that Suppress Excitatory Neuronal Activity Ex Vivo.

ACS chemical neuroscience·2024
Same author

One-stage surgical case management of a two-year-old Arabian horse affected by male-pseudo hermaphroditism.

Journal of equine veterinary science·2024
Same author

Expanding the genotype-phenotype spectrum in SCN8A-related disorders.

BMC neurology·2024
Same author

Expanding the genotype-phenotype spectrum in SCN8A-related disorders.

Research square·2023

Related Experiment Video

Updated: Jul 16, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Rotational movement during cyclic nucleotide-gated channel opening.

J P Johnson1, W N Zagotta

  • 1Howard Hughes Medical Institute & Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle 98195, USA.

Nature
|August 31, 2001
PubMed
Summary

Nickel ions (Ni2+) modulate cyclic nucleotide-gated (CNG) channels, essential for sensory signaling. Specific histidine residues in the C-linker region dictate whether Ni2+ potentiates or inhibits channel activity, revealing insights into gating mechanisms.

More Related Videos

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy
08:55

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: February 17, 2023

Related Experiment Videos

Last Updated: Jul 16, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels
11:19

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy
08:55

Single-Molecule Imaging of Lateral Mobility and Ion Channel Activity in Lipid Bilayers using Total Internal Reflection Fluorescence (TIRF) Microscopy

Published on: February 17, 2023

Area of Science:

  • Ion channel function
  • Molecular biology
  • Neuroscience

Background:

  • Cyclic nucleotide-gated (CNG) channels are vital for sensory transduction in vision, olfaction, and taste.
  • These channels regulate membrane potential and intracellular calcium (Ca2+) levels by responding to cyclic nucleotides.
  • Cytosolic nickel ions (Ni2+) exhibit differential effects on CNG channel subtypes, potentiating rod (CNG1) and inhibiting olfactory (CNG2) channels.

Purpose of the Study:

  • To investigate the role of specific histidine residues in the C-linker region of the CNG1 channel in mediating Ni2+ modulation.
  • To elucidate the structural basis for the differential effects of Ni2+ on CNG channel activity.

Main Methods:

  • Histidine scanning mutagenesis of the CNG1 channel's C-linker region.
  • Electrophysiological recordings to assess channel activity and response to Ni2+.

Main Results:

  • Identified distinct 'stripes' of histidine residues within the C-linker that confer either Ni2+ potentiation or Ni2+ inhibition.
  • These functional sites are spatially organized with a separation of approximately 50 degrees on an alpha-helix.
  • The findings support a model where Ni2+ coordination by specific histidines influences channel gating.

Conclusions:

  • The C-linker region of CNG channels contains key residues that dictate Ni2+ interaction and functional outcomes.
  • A conformational change involving rotation of the post-S6 region around the channel axis likely underlies Ni2+-mediated gating.
  • This mechanism provides a framework for understanding how subunit interactions regulate S6 movement and pore opening in CNG channels.