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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
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The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
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A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
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Calcium binding and voltage gating in Cx46 hemichannels.

Bernardo I Pinto1, Amaury Pupo1, Isaac E García1,2

  • 1Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso, Chile.

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|November 22, 2017
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Calcium and voltage allosterically regulate connexin (Cx) hemichannels. Calcium binding stabilizes the closed state, preventing ion flow and inhibiting water flux through Cx46 hemichannels.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Physiology

Background:

  • Connexin (Cx) hemichannels are crucial membrane proteins regulated by ions and voltage.
  • Calcium (Ca2+) and membrane voltage are key regulators of hemichannel gating.
  • Previous studies suggest Ca2+ stabilizes the closed state, but the precise mechanism remains unclear.

Purpose of the Study:

  • To elucidate the allosteric interplay between calcium and voltage in regulating Cx46 hemichannel gating.
  • To investigate the structural and functional consequences of Ca2+ binding on hemichannel conformation and ion/water flux.

Main Methods:

  • Electrophysiology to measure channel activity and kinetics.
  • Atomic force microscopy to visualize structural changes.
  • Development of an allosteric kinetic model to simulate channel behavior.

Main Results:

  • Ca2+ binding stabilizes the closed state of Cx46 hemichannels, acting via an electrostatic seal without major structural changes.
  • Apparent Ca2+ sensitivity increases with more negative membrane voltage.
  • Voltage sensor movement and Ca2+ binding are allosterically coupled, with Ca2+ reducing the energy for voltage sensor deactivation.
  • Ca2+ inhibits water flux, consistent with a pore-narrowing conformational change.

Conclusions:

  • Ca2+ and voltage act synergistically and allosterically to stabilize the closed conformation of Cx46 hemichannels.
  • The findings provide a mechanistic understanding of hemichannel regulation by divalent cations and membrane potential.
  • This regulation impacts ion and water transport across cell membranes.