Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/225551 |
Resumo: | Protein disulfde isomerases (PDIs) support endoplasmic reticulum redox protein folding and cellsurface thiol-redox control of thrombosis and vascular remodeling. The family prototype PDIA1 regulates NADPH oxidase signaling and cytoskeleton organization, however the related underlying mechanisms are unclear. Here we show that genes encoding human PDIA1 and its two paralogs PDIA8 and PDIA2 are each fanked by genes encoding Rho guanine-dissociation inhibitors (GDI), known regulators of RhoGTPases/cytoskeleton. Evolutionary histories of these three microsyntenic regions reveal their emergence by two successive duplication events of a primordial gene pair in the last common vertebrate ancestor. The arrangement, however, is substantially older, detectable in echinoderms, nematodes, and cnidarians. Thus, PDI/RhoGDI pairing in the same transcription orientation emerged early in animal evolution and has been largely maintained. PDI/RhoGDI pairs are embedded into conserved genomic regions displaying common cis-regulatory elements. Analysis of gene expression datasets supports evidence for PDI/RhoGDI coexpression in developmental/ infammatory contexts. PDIA1/RhoGDIα were co-induced in endothelial cells upon CRISP-R-promoted transcription activation of each pair component, and also in mouse arterial intima during fow-induced remodeling. We provide evidence for physical interaction between both proteins. These data support strong functional links between PDI and RhoGDI families, which likely maintained PDI/RhoGDI microsynteny along>800-million years of evolution. |
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Moretti, Ana I. S.Pavanelli, Jessyca C.Nolasco, PatríciaLeisegang, Mathias S.Tanaka, Leonardo Y.Fernandes, Carolina GonçalvesWosniak Jr., JoãoKajihara, DanielaDias, Matheus H.Fernandes, Denise C.Jo, HanjoongTran, Neoc-VinhEbersberger, IngoBrandes, Ralf P.Bonatto, DiegoLaurindo, Francisco R. M.2021-08-11T04:48:30Z20172045-2322http://hdl.handle.net/10183/225551001070780Protein disulfde isomerases (PDIs) support endoplasmic reticulum redox protein folding and cellsurface thiol-redox control of thrombosis and vascular remodeling. The family prototype PDIA1 regulates NADPH oxidase signaling and cytoskeleton organization, however the related underlying mechanisms are unclear. Here we show that genes encoding human PDIA1 and its two paralogs PDIA8 and PDIA2 are each fanked by genes encoding Rho guanine-dissociation inhibitors (GDI), known regulators of RhoGTPases/cytoskeleton. Evolutionary histories of these three microsyntenic regions reveal their emergence by two successive duplication events of a primordial gene pair in the last common vertebrate ancestor. The arrangement, however, is substantially older, detectable in echinoderms, nematodes, and cnidarians. Thus, PDI/RhoGDI pairing in the same transcription orientation emerged early in animal evolution and has been largely maintained. PDI/RhoGDI pairs are embedded into conserved genomic regions displaying common cis-regulatory elements. Analysis of gene expression datasets supports evidence for PDI/RhoGDI coexpression in developmental/ infammatory contexts. PDIA1/RhoGDIα were co-induced in endothelial cells upon CRISP-R-promoted transcription activation of each pair component, and also in mouse arterial intima during fow-induced remodeling. We provide evidence for physical interaction between both proteins. These data support strong functional links between PDI and RhoGDI families, which likely maintained PDI/RhoGDI microsynteny along>800-million years of evolution.application/pdfengScientific reports. London. Vol. 7, (Dec. 2017), 17262, 1-18 p.Inibidores de dissulfeto isomeraseInibidores de guanina dissódicaConserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor FamiliesEstrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001070780.pdf.txt001070780.pdf.txtExtracted Texttext/plain89741http://www.lume.ufrgs.br/bitstream/10183/225551/2/001070780.pdf.txte7f9e4be4dc7effeb61febab4b556ebeMD52ORIGINAL001070780.pdfTexto completo (inglês)application/pdf5042982http://www.lume.ufrgs.br/bitstream/10183/225551/1/001070780.pdf2d88747b2400285fec5b7fb2b61e7c0eMD5110183/2255512021-08-18 04:46:38.626762oai:www.lume.ufrgs.br:10183/225551Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2021-08-18T07:46:38Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
title |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
spellingShingle |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families Moretti, Ana I. S. Inibidores de dissulfeto isomerase Inibidores de guanina dissódica |
title_short |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
title_full |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
title_fullStr |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
title_full_unstemmed |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
title_sort |
Conserved gene microsynteny unveils functional interaction between protein disulfide isomerase and Rho Guanine-Dissociation Inhibitor Families |
author |
Moretti, Ana I. S. |
author_facet |
Moretti, Ana I. S. Pavanelli, Jessyca C. Nolasco, Patrícia Leisegang, Mathias S. Tanaka, Leonardo Y. Fernandes, Carolina Gonçalves Wosniak Jr., João Kajihara, Daniela Dias, Matheus H. Fernandes, Denise C. Jo, Hanjoong Tran, Neoc-Vinh Ebersberger, Ingo Brandes, Ralf P. Bonatto, Diego Laurindo, Francisco R. M. |
author_role |
author |
author2 |
Pavanelli, Jessyca C. Nolasco, Patrícia Leisegang, Mathias S. Tanaka, Leonardo Y. Fernandes, Carolina Gonçalves Wosniak Jr., João Kajihara, Daniela Dias, Matheus H. Fernandes, Denise C. Jo, Hanjoong Tran, Neoc-Vinh Ebersberger, Ingo Brandes, Ralf P. Bonatto, Diego Laurindo, Francisco R. M. |
author2_role |
author author author author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Moretti, Ana I. S. Pavanelli, Jessyca C. Nolasco, Patrícia Leisegang, Mathias S. Tanaka, Leonardo Y. Fernandes, Carolina Gonçalves Wosniak Jr., João Kajihara, Daniela Dias, Matheus H. Fernandes, Denise C. Jo, Hanjoong Tran, Neoc-Vinh Ebersberger, Ingo Brandes, Ralf P. Bonatto, Diego Laurindo, Francisco R. M. |
dc.subject.por.fl_str_mv |
Inibidores de dissulfeto isomerase Inibidores de guanina dissódica |
topic |
Inibidores de dissulfeto isomerase Inibidores de guanina dissódica |
description |
Protein disulfde isomerases (PDIs) support endoplasmic reticulum redox protein folding and cellsurface thiol-redox control of thrombosis and vascular remodeling. The family prototype PDIA1 regulates NADPH oxidase signaling and cytoskeleton organization, however the related underlying mechanisms are unclear. Here we show that genes encoding human PDIA1 and its two paralogs PDIA8 and PDIA2 are each fanked by genes encoding Rho guanine-dissociation inhibitors (GDI), known regulators of RhoGTPases/cytoskeleton. Evolutionary histories of these three microsyntenic regions reveal their emergence by two successive duplication events of a primordial gene pair in the last common vertebrate ancestor. The arrangement, however, is substantially older, detectable in echinoderms, nematodes, and cnidarians. Thus, PDI/RhoGDI pairing in the same transcription orientation emerged early in animal evolution and has been largely maintained. PDI/RhoGDI pairs are embedded into conserved genomic regions displaying common cis-regulatory elements. Analysis of gene expression datasets supports evidence for PDI/RhoGDI coexpression in developmental/ infammatory contexts. PDIA1/RhoGDIα were co-induced in endothelial cells upon CRISP-R-promoted transcription activation of each pair component, and also in mouse arterial intima during fow-induced remodeling. We provide evidence for physical interaction between both proteins. These data support strong functional links between PDI and RhoGDI families, which likely maintained PDI/RhoGDI microsynteny along>800-million years of evolution. |
publishDate |
2017 |
dc.date.issued.fl_str_mv |
2017 |
dc.date.accessioned.fl_str_mv |
2021-08-11T04:48:30Z |
dc.type.driver.fl_str_mv |
Estrangeiro info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
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article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/225551 |
dc.identifier.issn.pt_BR.fl_str_mv |
2045-2322 |
dc.identifier.nrb.pt_BR.fl_str_mv |
001070780 |
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2045-2322 001070780 |
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http://hdl.handle.net/10183/225551 |
dc.language.iso.fl_str_mv |
eng |
language |
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dc.relation.ispartof.pt_BR.fl_str_mv |
Scientific reports. London. Vol. 7, (Dec. 2017), 17262, 1-18 p. |
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info:eu-repo/semantics/openAccess |
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openAccess |
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