RhoA GTPase and F-actin Dynamically Regulate the Permeability of Cx43-made Channels in Rat Cardiac Myocytes

Gap junctions are clusters of transmembrane channels allowing a passive diffusion of ions and small molecules between adjacent cells. Connexin43, the main channel-forming protein expressed in ventricular myocytes, can associate with zonula occludens-1, a scaffolding protein linked to the actin cytos...

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Veröffentlicht in:The Journal of biological chemistry 2008-11, Vol.283 (45), p.30754-30765
Hauptverfasser: Derangeon, Mickaël, Bourmeyster, Nicolas, Plaisance, Isabelle, Pinet-Charvet, Caroline, Chen, Qian, Duthe, Fabien, Popoff, Michel R., Sarrouilhe, Denis, Hervé, Jean-Claude
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container_end_page 30765
container_issue 45
container_start_page 30754
container_title The Journal of biological chemistry
container_volume 283
creator Derangeon, Mickaël
Bourmeyster, Nicolas
Plaisance, Isabelle
Pinet-Charvet, Caroline
Chen, Qian
Duthe, Fabien
Popoff, Michel R.
Sarrouilhe, Denis
Hervé, Jean-Claude
description Gap junctions are clusters of transmembrane channels allowing a passive diffusion of ions and small molecules between adjacent cells. Connexin43, the main channel-forming protein expressed in ventricular myocytes, can associate with zonula occludens-1, a scaffolding protein linked to the actin cytoskeleton and to signal transduction molecules. The possible influence of Rho GTPases, major regulators of cellular junctions and of the actin cytoskeleton, in the modulation of gap junctional intercellular communication (GJIC) was examined. The activation of RhoA by cytoxic necrotizing factor 1 markedly enhanced GJIC, whereas its specific inhibition by the Clostridium botulinum C3 exoenzyme significantly reduced it. RhoA activity affects GJIC without major cellular redistribution of junctional plaques or changes in the Cx43 phosphorylation pattern. As these GTPases frequently act via the cortical cytoskeleton, the importance of F-actin in the modulation of GJIC was investigated by means of agents interfering with actin polymerization. Cytoskeleton stabilization by phalloidin slowed down the kinetics of channel rundown in the absence of ATP, whereas its disruption by cytochalasin D rapidly and markedly reduced GJIC despite ATP presence. Cytoskeleton stabilization by phalloidin markedly reduced the consequences of RhoA activation or inactivation. This mechanism appears to be the first described capable to both up- or down-regulate GJIC through RhoA activation or, conversely, inhibition. The inhibition of Rho downstream kinase effectors had no effect on GJIC. The present results provide further insight into the gating and regulation of junctional channels and identify a new downstream target for the small G-protein RhoA.
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Connexin43, the main channel-forming protein expressed in ventricular myocytes, can associate with zonula occludens-1, a scaffolding protein linked to the actin cytoskeleton and to signal transduction molecules. The possible influence of Rho GTPases, major regulators of cellular junctions and of the actin cytoskeleton, in the modulation of gap junctional intercellular communication (GJIC) was examined. The activation of RhoA by cytoxic necrotizing factor 1 markedly enhanced GJIC, whereas its specific inhibition by the Clostridium botulinum C3 exoenzyme significantly reduced it. RhoA activity affects GJIC without major cellular redistribution of junctional plaques or changes in the Cx43 phosphorylation pattern. As these GTPases frequently act via the cortical cytoskeleton, the importance of F-actin in the modulation of GJIC was investigated by means of agents interfering with actin polymerization. Cytoskeleton stabilization by phalloidin slowed down the kinetics of channel rundown in the absence of ATP, whereas its disruption by cytochalasin D rapidly and markedly reduced GJIC despite ATP presence. Cytoskeleton stabilization by phalloidin markedly reduced the consequences of RhoA activation or inactivation. This mechanism appears to be the first described capable to both up- or down-regulate GJIC through RhoA activation or, conversely, inhibition. The inhibition of Rho downstream kinase effectors had no effect on GJIC. 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subjects Actins - metabolism
Adenosine Triphosphate - metabolism
ADP Ribose Transferases - pharmacology
Animals
Bacterial Toxins - pharmacology
Botulinum Toxins - pharmacology
Cell Membrane Permeability - drug effects
Cell Membrane Permeability - physiology
Connexin 43 - metabolism
Cytochalasin D - pharmacology
Cytoskeleton - metabolism
Enzyme Activation - drug effects
Enzyme Activation - physiology
Escherichia coli Proteins - pharmacology
Gap Junctions - metabolism
Kinetics
Life Sciences
Mechanisms of Signal Transduction
Membrane Proteins - metabolism
Myocytes, Cardiac - metabolism
Nucleic Acid Synthesis Inhibitors - pharmacology
Phalloidine - pharmacology
Phosphoproteins - metabolism
Phosphorylation - drug effects
Phosphorylation - physiology
Poisons - pharmacology
Rats
rhoA GTP-Binding Protein - metabolism
Signal Transduction - drug effects
Signal Transduction - physiology
Zonula Occludens-1 Protein
title RhoA GTPase and F-actin Dynamically Regulate the Permeability of Cx43-made Channels in Rat Cardiac Myocytes
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