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

Gap Junctions01:37

Gap Junctions

Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
Non-gated Ion Channels01:24

Non-gated Ion Channels

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.
Non-gated Ion Channels01:24

Non-gated Ion Channels

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.
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

N-terminal pyroglutamylation of an HLA-A24-restricted immunodominant epitope enhances SARS-CoV-2-specific T-cell responses.

Frontiers in immunology·2026
Same author

The 2<sup>nd</sup> Asian Genetics Consortium Conference 2025 (AGCC 2025) -Genetics in Asia: Heredity, Diversity, Discovery, and Beyond.

Genes & genetic systems·2026
Same author

A Gly-to-Ala Substitution Confers Choline Phosphotransferase Activity on the CDP-Ethanolamine-Specific Mammalian EPT1.

Genes to cells : devoted to molecular & cellular mechanisms·2026
Same author

The three-dimensional structure of a proton-pumping pathway, the H-pathway, is evolutionarily conserved in all three families of cytochrome <i>c</i> oxidase.

Frontiers in chemistry·2026
Same author

Correction: Evolution of primate T-cell leukemia virus type 1 accessory genes and functional divergence of its antisense proteins.

PLoS pathogens·2025
Same author

Molecular basis of potent antiviral HLA-C-restricted CD8<sup>+</sup> T cell response to an immunodominant SARS-CoV-2 nucleocapsid epitope.

Nature communications·2025

Related Experiment Video

Updated: Jun 12, 2026

Modeling Biological Membranes with Circuit Boards and Measuring Electrical Signals in Axons: Student Laboratory Exercises
13:56

Modeling Biological Membranes with Circuit Boards and Measuring Electrical Signals in Axons: Student Laboratory Exercises

Published on: January 18, 2011

Structural and functional studies of gap junction channels.

So Nakagawa1, Shoji Maeda, Tomitake Tsukihara

  • 1Institute for Protein Research, Osaka University, OLABB, 6-2-3 Furuedai, Suita 565-0874, Japan.

Current Opinion in Structural Biology
|June 15, 2010
PubMed
Summary

Structural details of the human connexin26 gap junction channel

Area of Science:

  • Structural biology
  • Cell biology
  • Biophysics

Background:

  • Gap junction channels mediate intercellular communication and adhesion.
  • Connexin26 (Cx26) forms gap junction channels crucial for various tissues.
  • Understanding the open state structure of Cx26 channels is vital for elucidating their function.

Purpose of the Study:

  • To determine the high-resolution structure of the human connexin26 gap junction channel in its open state.
  • To elucidate the structural basis of the channel's gating mechanism.
  • To provide insights into the role of Cx26 channels in cell-cell interactions.

Main Methods:

  • X-ray crystallography was employed to analyze the human connexin26 gap junction channel.
  • Structural analysis focused on the arrangement of protomers and hemichannels.

More Related Videos

Single-cell Microinjection for Cell Communication Analysis
09:59

Single-cell Microinjection for Cell Communication Analysis

Published on: February 26, 2017

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
10:46

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Published on: July 16, 2013

Related Experiment Videos

Last Updated: Jun 12, 2026

Modeling Biological Membranes with Circuit Boards and Measuring Electrical Signals in Axons: Student Laboratory Exercises
13:56

Modeling Biological Membranes with Circuit Boards and Measuring Electrical Signals in Axons: Student Laboratory Exercises

Published on: January 18, 2011

Single-cell Microinjection for Cell Communication Analysis
09:59

Single-cell Microinjection for Cell Communication Analysis

Published on: February 26, 2017

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells
10:46

Mechanical Stimulation-induced Calcium Wave Propagation in Cell Monolayers: The Example of Bovine Corneal Endothelial Cells

Published on: July 16, 2013

  • The folding pattern of the connexin26 protomer and its amino-terminal region was investigated.

    • Main Results:

    • The open state structure reveals a six-fold symmetry, with each hemichannel composed of six protomers.
    • Each protomer adopts a four-helix bundle fold.
    • The amino-terminal region forms a funnel-like structure within the channel lumen, potentially involved in gating.

    Conclusions:

    • The determined structure provides atomic-level insights into the open state of the human connexin26 gap junction channel.
    • The amino-terminal region's structure offers a plausible explanation for the channel's gating mechanism.
    • The extensive interactions between hemichannels highlight the role of connexin26 gap junctions in maintaining cell-cell connections and adhesion.