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Related Experiment Videos

Conformational changes in surface structures of isolated connexin 26 gap junctions.

Daniel J Müller1, Galen M Hand, Andreas Engel

  • 1Max Planck Institute of Molecular Cell Biology and Genetics and BIOTEC, Technical University Dresden, Dresden, Germany. mueller@mpi-cbg.de

The EMBO Journal
|July 12, 2002
PubMed
Summary

Atomic force microscopy revealed how connexin 26 gap junction channels change shape. Calcium ions cause significant structural alterations in both cytoplasmic and extracellular domains, impacting cell communication.

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Area of Science:

  • Biophysics
  • Cell Biology
  • Structural Biology

Background:

  • Gap junction channels are crucial for intercellular communication.
  • Connexin 26 forms these channels, and their structure and function are key to understanding cell-to-cell signaling.

Purpose of the Study:

  • To visualize the conformational changes of connexin 26 gap junction plaques at submolecular resolution.
  • To investigate the role of calcium ions in modulating gap junction structure and function.

Main Methods:

  • Atomic Force Microscopy (AFM) was employed to image the cytoplasmic and extracellular surfaces of native connexin 26 gap junction plaques.
  • Submolecular resolution imaging allowed detailed observation of structural features and conformational dynamics.

Main Results:

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  • The cytoplasmic domains exhibit flexibility and can reversibly collapse under applied force.
  • Calcium ions induce a significant reduction in the extracellular channel entrance diameter (1.5 to 0.6 nm) and promote cytoplasmic microdomain formation.
  • These calcium-induced changes increase the overall plaque height, indicating structural modulation of both hemichannels and intact channels.

Conclusions:

  • Connexin 26 gap junctions undergo dynamic conformational changes in response to mechanical force and calcium ions.
  • Calcium ions play a critical role in regulating the structure and potentially the function of gap junction channels, affecting cell-cell contacts.