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Atomic force microscopy of arthropod gap junctions

S A John1, D Saner, J D Pitts

  • 1UCLA Cardiovascular Research Laboratory, UCLA School of Medicine 90095, USA. sjohn@ephys.ucla.edu

Journal of Structural Biology
|November 14, 1997
PubMed
Summary
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Atomic force microscopy revealed the structure of gap junctions from the Norway lobster. These junctions, composed of ductin protein, show a hexagonal lattice of particles similar to vertebrate connexon channels.

Area of Science:

  • Biophysics
  • Cell Biology
  • Structural Biology

Background:

  • Gap junctions facilitate intercellular communication.
  • Ductin is the major polypeptide in crustacean gap junctions.
  • Previous studies characterized vertebrate gap junction structure.

Purpose of the Study:

  • To characterize the structure of gap junctions from Nephrops norvegicus using Atomic Force Microscopy (AFM).
  • To investigate the substructure of gap junctions on both extracellular and cytoplasmic faces.
  • To compare the structure of invertebrate gap junctions with vertebrate connexon channels.

Main Methods:

  • Isolation of gap junctions from the hepatopancreas of Nephrops norvegicus.
  • High-resolution Atomic Force Microscopy (AFM) imaging in phosphate-buffered saline.

Related Experiment Videos

  • Force dissection to remove one membrane layer and expose underlying structures.
  • Fourier analysis of AFM images to determine particle arrangement and subunit composition.

    • Main Results:

    • Hydrated gap junctions appeared as 14 nm thick membrane plaques.
    • Force dissection revealed a 2 nm gap between apposing membranes.
    • High-resolution AFM showed particles arranged in a hexagonal lattice (a = b = 8.9 nm) on both faces.
    • Particles had a diameter of ~6.5 nm with a central pore-like depression, suggesting six subunits per particle.
    • Detailed substructure on the cytoplasmic face of hydrated gap junctions was visualized for the first time.

    Conclusions:

    • The structure of Nephrops norvegicus gap junctions, including particle arrangement and subunit composition, is highly similar to vertebrate connexon channels.
    • AFM provides high-resolution structural insights into invertebrate gap junctions.
    • Ductin-based gap junctions share conserved structural features with connexins, suggesting a common evolutionary origin.