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

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...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
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 include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
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 include the...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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 organs,...
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

A New Chapter for Genes, Chromosomes and Cancer.

Genes, chromosomes & cancer·2026
Same author

Restoration of CPAK type in total knee arthroplasty does not lead to superior clinical outcome: A study based on arthroplasty registry data.

Knee surgery, sports traumatology, arthroscopy : official journal of the ESSKA·2026
Same author

Learning planetary health through international & interprofessional education: a qualitative study of student reflections.

Medical education online·2026
Same author

The price of equality: determinants of the convergence in delivery costs in Bangladesh.

Frontiers in public health·2026
Same author

Transcriptional interference revisited.

Nature genetics·2026
Same author

Protonation-dependent substrate release in a bacterial homolog of vesicular glutamate.

Biophysical journal·2026
Same journal

Autosomal Dominant Tubulointerstitial Kidney Disease: My Kingdom for a Biomarker.

Journal of the American Society of Nephrology : JASN·2026
Same journal

Beyond the Margin: Improving Noninferiority Trials of Kidney Transplant Immunosuppression.

Journal of the American Society of Nephrology : JASN·2026
Same journal

Parathyroid Hormone Receptor 1 Facilitates Cyst Growth in Genetic Models of Autosomal Dominant Polycystic Kidney Disease.

Journal of the American Society of Nephrology : JASN·2026
Same journal

Alanyl-tRNA Synthetase 1 and Cyst Growth in Autosomal Dominant Polycystic Kidney Disease.

Journal of the American Society of Nephrology : JASN·2026
Same journal

Evaluating Barriers to Kidney Transplantation in the United States.

Journal of the American Society of Nephrology : JASN·2026
Same journal

Comparing Catheters to Fistulas in Older Patients Starting Hemodialysis (ACCESS HD).

Journal of the American Society of Nephrology : JASN·2026
See all related articles

Related Experiment Video

Updated: Jun 12, 2026

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

Barttin activates ClC-K channel function by modulating gating.

Martin Fischer1, Audrey G H Janssen, Christoph Fahlke

  • 1Institut für Neurophysiologie, Medizinische Hochschule Hannover, Hannover, Germany.

Journal of the American Society of Nephrology : JASN
|June 12, 2010
PubMed
Summary
This summary is machine-generated.

Barttin, an accessory protein, modulates ClC-K chloride channel gating, enhancing chloride transport in kidney and inner ear epithelia. It alters cooperative gating, crucial for epithelial ClC channel function.

More Related Videos

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

Measurement of Ion Concentration in the Unstirred Boundary Layer with Open Patch-Clamp Pipette: Implications in Control of Ion Channels by Fluid Flow
05:42

Measurement of Ion Concentration in the Unstirred Boundary Layer with Open Patch-Clamp Pipette: Implications in Control of Ion Channels by Fluid Flow

Published on: January 7, 2019

Related Experiment Videos

Last Updated: Jun 12, 2026

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

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

Measurement of Ion Concentration in the Unstirred Boundary Layer with Open Patch-Clamp Pipette: Implications in Control of Ion Channels by Fluid Flow
05:42

Measurement of Ion Concentration in the Unstirred Boundary Layer with Open Patch-Clamp Pipette: Implications in Control of Ion Channels by Fluid Flow

Published on: January 7, 2019

Area of Science:

  • Molecular Biology
  • Ion Channel Physiology
  • Epithelial Transport

Background:

  • Barttin is an accessory subunit of ClC-K chloride channels.
  • ClC-K channels are vital for renal and inner ear epithelia.
  • These channels possess a unique double-barreled structure with two protopores.

Purpose of the Study:

  • To investigate the role of barttin in the gating mechanisms of rat ClC-K1 and human ClC-Ka channels.
  • To elucidate how barttin influences the stability, distribution, and voltage-dependent gating of ClC-K channels.
  • To understand the functional implications of barttin on chloride flux in epithelial tissues.

Main Methods:

  • Heterologous expression of ClC-K channels and barttin in mammalian cells.
  • Patch-clamp recordings to analyze channel gating kinetics and voltage dependence.
  • Single-channel recordings to characterize protopore and common gating processes.

Main Results:

  • Rat ClC-K1 channels exhibit distinct fast and slow gating processes in the absence of barttin.
  • Barttin coexpression leads to voltage-independent common gating, increasing channel activity at physiological potentials.
  • Human ClC-Ka channels require barttin for function, displaying fast protopore gating without cooperative steps.

Conclusions:

  • Barttin significantly modifies the cooperative gating of double-barreled ClC-K channels.
  • Barttin enhances chloride flux through ClC-K channels by regulating gating.
  • This study highlights the physiological importance of barttin in epithelial ClC chloride channel gating.