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Conformational changes in the human Cx43/GJA1 gap junction channel visualized using cryo-EM.

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Connexin 43 (Cx43) gap junction intercellular channels (GJIChs) adopt dynamic conformations. These structures reveal how N-terminal helix arrangements influence channel gating and pore size, impacting cellular communication.

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Area of Science:

  • Structural biology
  • Molecular biophysics
  • Cell biology

Background:

  • Connexin proteins form gap junction intercellular channels (GJIChs) essential for cell-to-cell communication.
  • Understanding Cx43 GJICh structure is crucial for elucidating its function and regulation.

Purpose of the Study:

  • To determine the cryo-electron microscopy structures of Cx43 GJICh.
  • To identify and characterize different conformational states of Cx43 GJICh.
  • To investigate the factors influencing Cx43 GJICh conformation and gating.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of purified Cx43 GJICh.
  • Analysis of channel conformations in detergents and lipid nanodiscs.
  • Investigating effects of cholesteryl hemisuccinates, C-terminal truncations, and pH on conformation.

Main Results:

  • Identified three N-terminal helix conformations: gate-covering (GCN), pore-lining (PLN), and flexible intermediate (FIN).
  • Observed shifts in conformational equilibrium influenced by specific chemical and structural modifications.
  • Demonstrated a link between protomer conformation, lipid occlusion, and varying pore sizes.
  • Revealed an α-to-π-helix transition in the first transmembrane helix, creating membrane side openings in FIN and PLN states.

Conclusions:

  • Cx43 GJICh exists in a dynamic equilibrium of multiple conformations.
  • N-terminal helix conformation and its transitions are key determinants of Cx43 channel gating and function.
  • Structural insights provide a basis for understanding Cx43 GJICh regulation and potential therapeutic targeting.