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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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. 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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M801556200</identifier><identifier>PMID: 18667438</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>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</subject><ispartof>The Journal of biological chemistry, 2008-11, Vol.283 (45), p.30754-30765</ispartof><rights>2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c590t-16fead5656f13566f995c1e5f667f43c2bd881f175c359da85fbe9f22e5b1bee3</citedby><cites>FETCH-LOGICAL-c590t-16fead5656f13566f995c1e5f667f43c2bd881f175c359da85fbe9f22e5b1bee3</cites><orcidid>0000-0002-7771-2802 ; 0000-0002-9563-5142 ; 0000-0002-7927-9643</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2662158/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2662158/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18667438$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-03445512$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Derangeon, Mickaël</creatorcontrib><creatorcontrib>Bourmeyster, Nicolas</creatorcontrib><creatorcontrib>Plaisance, Isabelle</creatorcontrib><creatorcontrib>Pinet-Charvet, Caroline</creatorcontrib><creatorcontrib>Chen, Qian</creatorcontrib><creatorcontrib>Duthe, Fabien</creatorcontrib><creatorcontrib>Popoff, Michel R.</creatorcontrib><creatorcontrib>Sarrouilhe, Denis</creatorcontrib><creatorcontrib>Hervé, Jean-Claude</creatorcontrib><title>RhoA GTPase and F-actin Dynamically Regulate the Permeability of Cx43-made Channels in Rat Cardiac Myocytes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><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.</description><subject>Actins - metabolism</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>ADP Ribose Transferases - pharmacology</subject><subject>Animals</subject><subject>Bacterial Toxins - pharmacology</subject><subject>Botulinum Toxins - pharmacology</subject><subject>Cell Membrane Permeability - drug effects</subject><subject>Cell Membrane Permeability - physiology</subject><subject>Connexin 43 - metabolism</subject><subject>Cytochalasin D - pharmacology</subject><subject>Cytoskeleton - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Enzyme Activation - physiology</subject><subject>Escherichia coli Proteins - pharmacology</subject><subject>Gap Junctions - metabolism</subject><subject>Kinetics</subject><subject>Life Sciences</subject><subject>Mechanisms of Signal Transduction</subject><subject>Membrane Proteins - metabolism</subject><subject>Myocytes, Cardiac - metabolism</subject><subject>Nucleic Acid Synthesis Inhibitors - pharmacology</subject><subject>Phalloidine - pharmacology</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Phosphorylation - physiology</subject><subject>Poisons - pharmacology</subject><subject>Rats</subject><subject>rhoA GTP-Binding Protein - metabolism</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>Zonula Occludens-1 Protein</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUtv1DAUhS0EokNhyxK86IZFBj9ij7NBGgXaIk1FNbQSO8txricueVR2OpB_j0cZUUDCC1u6_s65RzoIvaZkSckqf39X2eWVIlQIyQh5ghaUKJ5xQb89RQtCGM0KJtQJehHjHUknL-hzdEKVlKucqwX6vm2GNb64uTYRsOlrfJ4ZO_oef5x603lr2nbCW9g9tGYEPDaAryF0YCrf-nHCg8Plz5xnnakBl43pe2gjTvKtGXFpQu2NxVfTYKcR4kv0zJk2wqvje4puzz_dlJfZ5svF53K9yawoyJhR6cDUQgrpKBdSuqIQloJwKbPLuWVVrRR1dCUsF0VtlHAVFI4xEBWtAPgp-jD73j9UHdQW-jGYVt8H35kw6cF4_fdP7xu9G_aaScmoUMng3WzQ_CO7XG_0YUZ4ngtB2Z4mdjmzNgwxBnC_BZToQ0U6VaQfK0qCN3-me8SPnSTg7Ljd75ofPoCu_GAb6DRTXOdCc7ISecLezpgzgza74KO-_coI5YdNIt2JUDOROoG9h6Cj9dBbqJOpHXU9-P-F_AXUjLSa</recordid><startdate>20081107</startdate><enddate>20081107</enddate><creator>Derangeon, Mickaël</creator><creator>Bourmeyster, Nicolas</creator><creator>Plaisance, Isabelle</creator><creator>Pinet-Charvet, Caroline</creator><creator>Chen, Qian</creator><creator>Duthe, Fabien</creator><creator>Popoff, Michel R.</creator><creator>Sarrouilhe, Denis</creator><creator>Hervé, Jean-Claude</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7771-2802</orcidid><orcidid>https://orcid.org/0000-0002-9563-5142</orcidid><orcidid>https://orcid.org/0000-0002-7927-9643</orcidid></search><sort><creationdate>20081107</creationdate><title>RhoA GTPase and F-actin Dynamically Regulate the Permeability of Cx43-made Channels in Rat Cardiac Myocytes</title><author>Derangeon, Mickaël ; Bourmeyster, Nicolas ; Plaisance, Isabelle ; Pinet-Charvet, Caroline ; Chen, Qian ; Duthe, Fabien ; Popoff, Michel R. ; Sarrouilhe, Denis ; Hervé, Jean-Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c590t-16fead5656f13566f995c1e5f667f43c2bd881f175c359da85fbe9f22e5b1bee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Actins - metabolism</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>ADP Ribose Transferases - pharmacology</topic><topic>Animals</topic><topic>Bacterial Toxins - pharmacology</topic><topic>Botulinum Toxins - pharmacology</topic><topic>Cell Membrane Permeability - drug effects</topic><topic>Cell Membrane Permeability - physiology</topic><topic>Connexin 43 - metabolism</topic><topic>Cytochalasin D - pharmacology</topic><topic>Cytoskeleton - metabolism</topic><topic>Enzyme Activation - drug effects</topic><topic>Enzyme Activation - physiology</topic><topic>Escherichia coli Proteins - pharmacology</topic><topic>Gap Junctions - metabolism</topic><topic>Kinetics</topic><topic>Life Sciences</topic><topic>Mechanisms of Signal Transduction</topic><topic>Membrane Proteins - metabolism</topic><topic>Myocytes, Cardiac - metabolism</topic><topic>Nucleic Acid Synthesis Inhibitors - pharmacology</topic><topic>Phalloidine - pharmacology</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation - drug effects</topic><topic>Phosphorylation - physiology</topic><topic>Poisons - pharmacology</topic><topic>Rats</topic><topic>rhoA GTP-Binding Protein - metabolism</topic><topic>Signal Transduction - drug effects</topic><topic>Signal Transduction - physiology</topic><topic>Zonula Occludens-1 Protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Derangeon, Mickaël</creatorcontrib><creatorcontrib>Bourmeyster, Nicolas</creatorcontrib><creatorcontrib>Plaisance, Isabelle</creatorcontrib><creatorcontrib>Pinet-Charvet, Caroline</creatorcontrib><creatorcontrib>Chen, Qian</creatorcontrib><creatorcontrib>Duthe, Fabien</creatorcontrib><creatorcontrib>Popoff, Michel R.</creatorcontrib><creatorcontrib>Sarrouilhe, Denis</creatorcontrib><creatorcontrib>Hervé, Jean-Claude</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Derangeon, Mickaël</au><au>Bourmeyster, Nicolas</au><au>Plaisance, Isabelle</au><au>Pinet-Charvet, Caroline</au><au>Chen, Qian</au><au>Duthe, Fabien</au><au>Popoff, Michel R.</au><au>Sarrouilhe, Denis</au><au>Hervé, Jean-Claude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RhoA GTPase and F-actin Dynamically Regulate the Permeability of Cx43-made Channels in Rat Cardiac Myocytes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2008-11-07</date><risdate>2008</risdate><volume>283</volume><issue>45</issue><spage>30754</spage><epage>30765</epage><pages>30754-30765</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18667438</pmid><doi>10.1074/jbc.M801556200</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0002-7771-2802</orcidid><orcidid>https://orcid.org/0000-0002-9563-5142</orcidid><orcidid>https://orcid.org/0000-0002-7927-9643</orcidid><oa>free_for_read</oa></addata></record> |
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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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