Calcium binding and voltage gating in Cx46 hemichannels View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Bernardo I. Pinto, Amaury Pupo, Isaac E. García, Karel Mena-Ulecia, Agustín D. Martínez, Ramón Latorre, Carlos Gonzalez

ABSTRACT

The opening of connexin (Cx) hemichannels in the membrane is tightly regulated by calcium (Ca2+) and membrane voltage. Electrophysiological and atomic force microscopy experiments indicate that Ca2+ stabilizes the hemichannel closed state. However, structural data show that Ca2+ binding induces an electrostatic seal preventing ion transport without significant structural rearrangements. In agreement with the closed-state stabilization hypothesis, we found that the apparent Ca2+ sensitivity is increased as the voltage is made more negative. Moreover, the voltage and Ca2+ dependence of the channel kinetics indicate that the voltage sensor movement and Ca2+ binding are allosterically coupled. An allosteric kinetic model in which the Ca2+ decreases the energy necessary to deactivate the voltage sensor reproduces the effects of Ca2+ and voltage in Cx46 hemichannels. In agreement with the model and suggesting a conformational change that narrows the pore, Ca2+ inhibits the water flux through Cx hemichannels. We conclude that Ca2+ and voltage act allosterically to stabilize the closed conformation of Cx46 hemichannels. More... »

PAGES

15851

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-017-15975-5

DOI

http://dx.doi.org/10.1038/s41598-017-15975-5

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https://app.dimensions.ai/details/publication/pub.1092697012

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29158540


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44 schema:description The opening of connexin (Cx) hemichannels in the membrane is tightly regulated by calcium (Ca<sup>2+</sup>) and membrane voltage. Electrophysiological and atomic force microscopy experiments indicate that Ca<sup>2+</sup> stabilizes the hemichannel closed state. However, structural data show that Ca<sup>2+</sup> binding induces an electrostatic seal preventing ion transport without significant structural rearrangements. In agreement with the closed-state stabilization hypothesis, we found that the apparent Ca<sup>2+</sup> sensitivity is increased as the voltage is made more negative. Moreover, the voltage and Ca<sup>2+</sup> dependence of the channel kinetics indicate that the voltage sensor movement and Ca<sup>2+</sup> binding are allosterically coupled. An allosteric kinetic model in which the Ca<sup>2+</sup> decreases the energy necessary to deactivate the voltage sensor reproduces the effects of Ca<sup>2+</sup> and voltage in Cx46 hemichannels. In agreement with the model and suggesting a conformational change that narrows the pore, Ca<sup>2+</sup> inhibits the water flux through Cx hemichannels. We conclude that Ca<sup>2+</sup> and voltage act allosterically to stabilize the closed conformation of Cx46 hemichannels.
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