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Related Experiment Videos

Structure of gap junction intercellular channels

M Yeager1, B J Nicholson

  • 1Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA. yeager@scripps.edu

Current Opinion in Structural Biology
|April 1, 1996
PubMed
Summary
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Connexins form gap junctions, crucial for cell communication. Recent studies reveal the alpha-helical structure of these transmembrane channels, offering insights into their function and regulation.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Cell Biology

Background:

  • Gap junctions are protein channels facilitating intercellular communication.
  • Connexins, the protein family forming gap junctions, possess transmembrane domains and cytoplasmic termini.
  • Channel regulation involves C-terminal tails, pH, and phosphorylation, with cysteine residues stabilizing extracellular loops.

Purpose of the Study:

  • To elucidate the structural organization of connexin gap junctions.
  • To investigate the role of alpha helices in the transmembrane channel structure.
  • To detail connexin interactions within hemi-channels and connexon-connexon interactions.

Main Methods:

  • Electron cryocrystallography of truncated recombinant alpha 1 (Cx43) two-dimensional crystals.

Related Experiment Videos

  • Analysis of images from tilted crystals for three-dimensional structural determination.

    • Main Results:

    • The transmembrane boundary of the intercellular channel is lined with alpha helices.
    • A ring of alpha helices is situated at the interface with membrane lipids.
    • Structural details of connexin interactions within hemi-channels and connexon-connexon interactions are being revealed.

    Conclusions:

    • Connexin structure, particularly alpha-helical arrangements, is key to gap junction function.
    • Structural insights aid in understanding channel regulation and intercellular communication.
    • Further 3D analysis will provide comprehensive structural details of connexin channels.