The Cx43-like connexin protein Cx40.8 is differentially localized during fin ontogeny and fin regeneration
Connexins (Cx) are the subunits of gap junctions, membraneous protein channels that permit the exchange of small molecules between adjacent cells. Cx43 is required for cell proliferation in the zebrafish caudal fin. Previously, we found that a Cx43-like connexin, cx40.8, is co-expressed with cx43 in...
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description | Connexins (Cx) are the subunits of gap junctions, membraneous protein channels that permit the exchange of small molecules between adjacent cells. Cx43 is required for cell proliferation in the zebrafish caudal fin. Previously, we found that a Cx43-like connexin, cx40.8, is co-expressed with cx43 in the population of proliferating cells during fin regeneration. Here we demonstrate that Cx40.8 exhibits novel differential subcellular localization in vivo, depending on the growth status of the fin. During fin ontogeny, Cx40.8 is found at the plasma membrane, but Cx40.8 is retained in the Golgi apparatus during regeneration. We next identified a 30 amino acid domain of Cx40.8 responsible for its dynamic localization. One possible explanation for the differential localization is that Cx40.8 contributes to the regulation of Cx43 in vivo, perhaps modifying channel activity during ontogenetic growth. However, we find that the voltage-gating properties of Cx40.8 are similar to Cx43. Together our findings reveal that Cx40.8 exhibits differential subcellular localization in vivo, dependent on a discrete domain in its carboxy terminus. We suggest that the dynamic localization of Cx40.8 differentially influences Cx43-dependent cell proliferation during ontogeny and regeneration. |
doi_str_mv | 10.1371/journal.pone.0031364 |
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Cx43 is required for cell proliferation in the zebrafish caudal fin. Previously, we found that a Cx43-like connexin, cx40.8, is co-expressed with cx43 in the population of proliferating cells during fin regeneration. Here we demonstrate that Cx40.8 exhibits novel differential subcellular localization in vivo, depending on the growth status of the fin. During fin ontogeny, Cx40.8 is found at the plasma membrane, but Cx40.8 is retained in the Golgi apparatus during regeneration. We next identified a 30 amino acid domain of Cx40.8 responsible for its dynamic localization. One possible explanation for the differential localization is that Cx40.8 contributes to the regulation of Cx43 in vivo, perhaps modifying channel activity during ontogenetic growth. However, we find that the voltage-gating properties of Cx40.8 are similar to Cx43. Together our findings reveal that Cx40.8 exhibits differential subcellular localization in vivo, dependent on a discrete domain in its carboxy terminus. We suggest that the dynamic localization of Cx40.8 differentially influences Cx43-dependent cell proliferation during ontogeny and regeneration.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0031364</identifier><identifier>PMID: 22347467</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Animal Fins - chemistry ; Animal Fins - physiology ; Animals ; Biology ; Cell growth ; Cell Proliferation ; Channel gating ; Connexin 43 ; Connexins ; Connexins - metabolism ; Danio rerio ; Developmental biology ; Gap Junction alpha-5 Protein ; Gap junctions ; Genes ; Genomes ; Golgi apparatus ; Growth rate ; Influence ; Laboratories ; Liver diseases ; Localization ; Medicine ; Mutation ; Ontogeny ; Plasma ; Proteins ; Regeneration ; Rodents ; Spermatogenesis ; Zebrafish ; Zebrafish - metabolism ; Zebrafish Proteins - metabolism</subject><ispartof>PloS one, 2012-02, Vol.7 (2), p.e31364-e31364</ispartof><rights>COPYRIGHT 2012 Public Library of Science</rights><rights>2012 Gerhart et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Gerhart et al. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c757t-5092730e6178140d47ab6fc330b4d001f300326e08fdfbdc9c176cbf4eac0d3a3</citedby><cites>FETCH-LOGICAL-c757t-5092730e6178140d47ab6fc330b4d001f300326e08fdfbdc9c176cbf4eac0d3a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3275562/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3275562/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2095,2914,23846,27903,27904,53770,53772,79347,79348</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22347467$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Mueller, Ferenc</contributor><creatorcontrib>Gerhart, Sarah V</creatorcontrib><creatorcontrib>Eble, Diane M</creatorcontrib><creatorcontrib>Burger, R Michael</creatorcontrib><creatorcontrib>Oline, Stefan N</creatorcontrib><creatorcontrib>Vacaru, Ana</creatorcontrib><creatorcontrib>Sadler, Kirsten C</creatorcontrib><creatorcontrib>Jefferis, Rebecca</creatorcontrib><creatorcontrib>Iovine, M Kathryn</creatorcontrib><title>The Cx43-like connexin protein Cx40.8 is differentially localized during fin ontogeny and fin regeneration</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Connexins (Cx) are the subunits of gap junctions, membraneous protein channels that permit the exchange of small molecules between adjacent cells. Cx43 is required for cell proliferation in the zebrafish caudal fin. Previously, we found that a Cx43-like connexin, cx40.8, is co-expressed with cx43 in the population of proliferating cells during fin regeneration. Here we demonstrate that Cx40.8 exhibits novel differential subcellular localization in vivo, depending on the growth status of the fin. During fin ontogeny, Cx40.8 is found at the plasma membrane, but Cx40.8 is retained in the Golgi apparatus during regeneration. We next identified a 30 amino acid domain of Cx40.8 responsible for its dynamic localization. One possible explanation for the differential localization is that Cx40.8 contributes to the regulation of Cx43 in vivo, perhaps modifying channel activity during ontogenetic growth. However, we find that the voltage-gating properties of Cx40.8 are similar to Cx43. Together our findings reveal that Cx40.8 exhibits differential subcellular localization in vivo, dependent on a discrete domain in its carboxy terminus. We suggest that the dynamic localization of Cx40.8 differentially influences Cx43-dependent cell proliferation during ontogeny and regeneration.</description><subject>Amino acids</subject><subject>Animal Fins - chemistry</subject><subject>Animal Fins - physiology</subject><subject>Animals</subject><subject>Biology</subject><subject>Cell growth</subject><subject>Cell Proliferation</subject><subject>Channel gating</subject><subject>Connexin 43</subject><subject>Connexins</subject><subject>Connexins - metabolism</subject><subject>Danio rerio</subject><subject>Developmental biology</subject><subject>Gap Junction alpha-5 Protein</subject><subject>Gap junctions</subject><subject>Genes</subject><subject>Genomes</subject><subject>Golgi apparatus</subject><subject>Growth rate</subject><subject>Influence</subject><subject>Laboratories</subject><subject>Liver diseases</subject><subject>Localization</subject><subject>Medicine</subject><subject>Mutation</subject><subject>Ontogeny</subject><subject>Plasma</subject><subject>Proteins</subject><subject>Regeneration</subject><subject>Rodents</subject><subject>Spermatogenesis</subject><subject>Zebrafish</subject><subject>Zebrafish - 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chemistry</topic><topic>Animal Fins - physiology</topic><topic>Animals</topic><topic>Biology</topic><topic>Cell growth</topic><topic>Cell Proliferation</topic><topic>Channel gating</topic><topic>Connexin 43</topic><topic>Connexins</topic><topic>Connexins - metabolism</topic><topic>Danio rerio</topic><topic>Developmental biology</topic><topic>Gap Junction alpha-5 Protein</topic><topic>Gap junctions</topic><topic>Genes</topic><topic>Genomes</topic><topic>Golgi apparatus</topic><topic>Growth rate</topic><topic>Influence</topic><topic>Laboratories</topic><topic>Liver diseases</topic><topic>Localization</topic><topic>Medicine</topic><topic>Mutation</topic><topic>Ontogeny</topic><topic>Plasma</topic><topic>Proteins</topic><topic>Regeneration</topic><topic>Rodents</topic><topic>Spermatogenesis</topic><topic>Zebrafish</topic><topic>Zebrafish - metabolism</topic><topic>Zebrafish Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gerhart, Sarah V</creatorcontrib><creatorcontrib>Eble, Diane M</creatorcontrib><creatorcontrib>Burger, R Michael</creatorcontrib><creatorcontrib>Oline, Stefan N</creatorcontrib><creatorcontrib>Vacaru, Ana</creatorcontrib><creatorcontrib>Sadler, Kirsten C</creatorcontrib><creatorcontrib>Jefferis, Rebecca</creatorcontrib><creatorcontrib>Iovine, M Kathryn</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gerhart, Sarah V</au><au>Eble, Diane M</au><au>Burger, R Michael</au><au>Oline, Stefan N</au><au>Vacaru, Ana</au><au>Sadler, Kirsten C</au><au>Jefferis, Rebecca</au><au>Iovine, M Kathryn</au><au>Mueller, Ferenc</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Cx43-like connexin protein Cx40.8 is differentially localized during fin ontogeny and fin regeneration</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-02-08</date><risdate>2012</risdate><volume>7</volume><issue>2</issue><spage>e31364</spage><epage>e31364</epage><pages>e31364-e31364</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Connexins (Cx) are the subunits of gap junctions, membraneous protein channels that permit the exchange of small molecules between adjacent cells. Cx43 is required for cell proliferation in the zebrafish caudal fin. Previously, we found that a Cx43-like connexin, cx40.8, is co-expressed with cx43 in the population of proliferating cells during fin regeneration. Here we demonstrate that Cx40.8 exhibits novel differential subcellular localization in vivo, depending on the growth status of the fin. During fin ontogeny, Cx40.8 is found at the plasma membrane, but Cx40.8 is retained in the Golgi apparatus during regeneration. We next identified a 30 amino acid domain of Cx40.8 responsible for its dynamic localization. One possible explanation for the differential localization is that Cx40.8 contributes to the regulation of Cx43 in vivo, perhaps modifying channel activity during ontogenetic growth. However, we find that the voltage-gating properties of Cx40.8 are similar to Cx43. Together our findings reveal that Cx40.8 exhibits differential subcellular localization in vivo, dependent on a discrete domain in its carboxy terminus. We suggest that the dynamic localization of Cx40.8 differentially influences Cx43-dependent cell proliferation during ontogeny and regeneration.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>22347467</pmid><doi>10.1371/journal.pone.0031364</doi><tpages>e31364</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino acids Animal Fins - chemistry Animal Fins - physiology Animals Biology Cell growth Cell Proliferation Channel gating Connexin 43 Connexins Connexins - metabolism Danio rerio Developmental biology Gap Junction alpha-5 Protein Gap junctions Genes Genomes Golgi apparatus Growth rate Influence Laboratories Liver diseases Localization Medicine Mutation Ontogeny Plasma Proteins Regeneration Rodents Spermatogenesis Zebrafish Zebrafish - metabolism Zebrafish Proteins - metabolism |
title | The Cx43-like connexin protein Cx40.8 is differentially localized during fin ontogeny and fin regeneration |
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