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Quantifying electrostatic control of docking and binding energetics in functional Cx36 gap junctions.

Robert S Wong1, Zhiyuan Song2, Yu T Zheng1

  • 1Department of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada.

Communications Biology
|June 11, 2026
PubMed
Summary

Electrostatic interactions (ESIs) between connexin36 (Cx36) proteins are crucial for forming functional neuronal gap junctions (GJs). Specific ESIs ensure Cx36 proteins connect only with themselves, not other brain connexins.

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Biochemistry

Background:

  • Connexin36 (Cx36) forms neuronal gap junctions (GJs), or electrical synapses, essential for brain function.
  • High-resolution structures reveal electrostatic interactions (ESIs) between Cx36 hemichannels at extracellular loops, but their functional roles are unclear.

Purpose of the Study:

  • To investigate the mechanistic roles of ESIs in Cx36 GJ formation and specificity.
  • To determine the minimum number of ESIs required for functional GJ assembly.

Main Methods:

  • Designed missense variants targeting key Cx36 E2 interface residues.
  • Employed computational calculations and dual patch-clamp experiments in HEK293 cells.

Main Results:

  • At least three ESI pairs per E2-E2 interface are necessary for functional Cx36 GJ formation.
  • Cx36 ESIs contribute to homotypic docking specificity, preventing heterotypic GJs with other brain connexins.

Conclusions:

  • Cx36 GJ formation and specificity are governed by specific electrostatic interactions.
  • These findings offer molecular insights into connexin function and potential therapeutic targets for neurological diseases.