Conserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families

Abstract Protein disulfide isomerases (PDIs) support endoplasmic reticulum redox protein folding and cell-surface thiol-redox control of thrombosis and vascular remodeling. The family prototype PDIA1 regulates NADPH oxidase signaling and cytoskeleton organization, however the related underlying mech...

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Autores principales:	Ana I. S. Moretti, Jessyca C. Pavanelli, Patrícia Nolasco, Matthias S. Leisegang, Leonardo Y. Tanaka, Carolina G. Fernandes, João Wosniak, Daniela Kajihara, Matheus H. Dias, Denise C. Fernandes, Hanjoong Jo, Ngoc-Vinh Tran, Ingo Ebersberger, Ralf P. Brandes, Diego Bonatto, Francisco R. M. Laurindo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ecacaa9b61b844f7b39828427de7b836
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spelling	oai:doaj.org-article:ecacaa9b61b844f7b39828427de7b8362021-12-02T15:05:13ZConserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families10.1038/s41598-017-16947-52045-2322https://doaj.org/article/ecacaa9b61b844f7b39828427de7b8362017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-16947-5https://doaj.org/toc/2045-2322Abstract Protein disulfide isomerases (PDIs) support endoplasmic reticulum redox protein folding and cell-surface 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 flanked 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/inflammatory 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 flow-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.Ana I. S. MorettiJessyca C. PavanelliPatrícia NolascoMatthias S. LeisegangLeonardo Y. TanakaCarolina G. FernandesJoão WosniakDaniela KajiharaMatheus H. DiasDenise C. FernandesHanjoong JoNgoc-Vinh TranIngo EbersbergerRalf P. BrandesDiego BonattoFrancisco R. M. LaurindoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-18 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ana I. S. Moretti Jessyca C. Pavanelli Patrícia Nolasco Matthias S. Leisegang Leonardo Y. Tanaka Carolina G. Fernandes João Wosniak Daniela Kajihara Matheus H. Dias Denise C. Fernandes Hanjoong Jo Ngoc-Vinh Tran Ingo Ebersberger Ralf P. Brandes Diego Bonatto Francisco R. M. Laurindo Conserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families
description	Abstract Protein disulfide isomerases (PDIs) support endoplasmic reticulum redox protein folding and cell-surface 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 flanked 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/inflammatory 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 flow-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.
format	article
author	Ana I. S. Moretti Jessyca C. Pavanelli Patrícia Nolasco Matthias S. Leisegang Leonardo Y. Tanaka Carolina G. Fernandes João Wosniak Daniela Kajihara Matheus H. Dias Denise C. Fernandes Hanjoong Jo Ngoc-Vinh Tran Ingo Ebersberger Ralf P. Brandes Diego Bonatto Francisco R. M. Laurindo
author_facet	Ana I. S. Moretti Jessyca C. Pavanelli Patrícia Nolasco Matthias S. Leisegang Leonardo Y. Tanaka Carolina G. Fernandes João Wosniak Daniela Kajihara Matheus H. Dias Denise C. Fernandes Hanjoong Jo Ngoc-Vinh Tran Ingo Ebersberger Ralf P. Brandes Diego Bonatto Francisco R. M. Laurindo
author_sort	Ana I. S. Moretti
title	Conserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families
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
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ecacaa9b61b844f7b39828427de7b836
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Conserved Gene Microsynteny Unveils Functional Interaction Between Protein Disulfide Isomerase and Rho Guanine-Dissociation Inhibitor Families

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