A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia

Autores
Fiol, Diego Fernando; Sanmarti, Enio; Lim, Andreana H.; Kültz, Dietmar
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: Tilapia (Oreochromis mossambicus) are euryhaline fishes capable of tolerating large salinity changes. In a previous study aimed to identify genes involved in osmotolerance, we isolated an mRNA sequence with similarity to GRAIL (Gene Related to Anergy In Lymphocytes), which is a critical regulator of adaptive immunity and development. Tilapia GRAIL contains a PA (protease associated) domain and a C3H2C3 RING finger domain indicative of E3 ubiquitin ligase activity. Scope of review: Western blots analysis was used to assess GRAIL expression pattern and responses to hyperosmotic stress. Immunohistochemistry was used to reveal the cellular localization of GRAIL in gill epithelium. Overexpression in HEK293 T-Rex cells was used to functionally characterize tilapia GRAIL. Salinity stress causes strong up-regulation of both mRNA and protein levels of tilapia GRAIL in gill epithelium. Tissue distribution of GRAIL protein is mainly confined to gill epithelium, which is the primary tissue responsible for osmoregulation of teleost fishes. Overexpression of tilapia GRAIL in HEK293 cells increases cell survival (cell viability) while decreases apoptosis during salinity challenge. Major conclusions: Our data indicate that tilapia GRAIL is a novel E3 ubiquitin ligase involved in osmotic stress signaling, which promotes environmental salinity tolerance by supporting gill cell function during hyperosmotic stress. General significance: Involvement of tilapia GRAIL in the osmotic stress response suggests that GRAIL E3 ubiquitin ligases play a broader role in environmental stress responses, beyond their documented functions in adaptive immunity and development.
Fil: Fiol, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina. University Of California At Davis; Estados Unidos
Fil: Sanmarti, Enio. University Of California At Davis; Estados Unidos
Fil: Lim, Andreana H.. University Of California At Davis; Estados Unidos
Fil: Kültz, Dietmar. University Of California At Davis; Estados Unidos
Materia
Hyperosmotic Stress
Oreochromis Mossambicus
Grail
Greul
Goliath
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/13064

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spelling A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapiaFiol, Diego FernandoSanmarti, EnioLim, Andreana H.Kültz, DietmarHyperosmotic StressOreochromis MossambicusGrailGreulGoliathhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Background: Tilapia (Oreochromis mossambicus) are euryhaline fishes capable of tolerating large salinity changes. In a previous study aimed to identify genes involved in osmotolerance, we isolated an mRNA sequence with similarity to GRAIL (Gene Related to Anergy In Lymphocytes), which is a critical regulator of adaptive immunity and development. Tilapia GRAIL contains a PA (protease associated) domain and a C3H2C3 RING finger domain indicative of E3 ubiquitin ligase activity. Scope of review: Western blots analysis was used to assess GRAIL expression pattern and responses to hyperosmotic stress. Immunohistochemistry was used to reveal the cellular localization of GRAIL in gill epithelium. Overexpression in HEK293 T-Rex cells was used to functionally characterize tilapia GRAIL. Salinity stress causes strong up-regulation of both mRNA and protein levels of tilapia GRAIL in gill epithelium. Tissue distribution of GRAIL protein is mainly confined to gill epithelium, which is the primary tissue responsible for osmoregulation of teleost fishes. Overexpression of tilapia GRAIL in HEK293 cells increases cell survival (cell viability) while decreases apoptosis during salinity challenge. Major conclusions: Our data indicate that tilapia GRAIL is a novel E3 ubiquitin ligase involved in osmotic stress signaling, which promotes environmental salinity tolerance by supporting gill cell function during hyperosmotic stress. General significance: Involvement of tilapia GRAIL in the osmotic stress response suggests that GRAIL E3 ubiquitin ligases play a broader role in environmental stress responses, beyond their documented functions in adaptive immunity and development.Fil: Fiol, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina. University Of California At Davis; Estados UnidosFil: Sanmarti, Enio. University Of California At Davis; Estados UnidosFil: Lim, Andreana H.. University Of California At Davis; Estados UnidosFil: Kültz, Dietmar. University Of California At Davis; Estados UnidosElsevier Science2011-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/13064Fiol, Diego Fernando; Sanmarti, Enio; Lim, Andreana H.; Kültz, Dietmar; A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1810; 4; 4-2011; 439-4450304-4165enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0304416510002552info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2010.11.005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:46:07Zoai:ri.conicet.gov.ar:11336/13064instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 14:46:07.472CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
title A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
spellingShingle A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
Fiol, Diego Fernando
Hyperosmotic Stress
Oreochromis Mossambicus
Grail
Greul
Goliath
title_short A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
title_full A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
title_fullStr A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
title_full_unstemmed A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
title_sort A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia
dc.creator.none.fl_str_mv Fiol, Diego Fernando
Sanmarti, Enio
Lim, Andreana H.
Kültz, Dietmar
author Fiol, Diego Fernando
author_facet Fiol, Diego Fernando
Sanmarti, Enio
Lim, Andreana H.
Kültz, Dietmar
author_role author
author2 Sanmarti, Enio
Lim, Andreana H.
Kültz, Dietmar
author2_role author
author
author
dc.subject.none.fl_str_mv Hyperosmotic Stress
Oreochromis Mossambicus
Grail
Greul
Goliath
topic Hyperosmotic Stress
Oreochromis Mossambicus
Grail
Greul
Goliath
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Background: Tilapia (Oreochromis mossambicus) are euryhaline fishes capable of tolerating large salinity changes. In a previous study aimed to identify genes involved in osmotolerance, we isolated an mRNA sequence with similarity to GRAIL (Gene Related to Anergy In Lymphocytes), which is a critical regulator of adaptive immunity and development. Tilapia GRAIL contains a PA (protease associated) domain and a C3H2C3 RING finger domain indicative of E3 ubiquitin ligase activity. Scope of review: Western blots analysis was used to assess GRAIL expression pattern and responses to hyperosmotic stress. Immunohistochemistry was used to reveal the cellular localization of GRAIL in gill epithelium. Overexpression in HEK293 T-Rex cells was used to functionally characterize tilapia GRAIL. Salinity stress causes strong up-regulation of both mRNA and protein levels of tilapia GRAIL in gill epithelium. Tissue distribution of GRAIL protein is mainly confined to gill epithelium, which is the primary tissue responsible for osmoregulation of teleost fishes. Overexpression of tilapia GRAIL in HEK293 cells increases cell survival (cell viability) while decreases apoptosis during salinity challenge. Major conclusions: Our data indicate that tilapia GRAIL is a novel E3 ubiquitin ligase involved in osmotic stress signaling, which promotes environmental salinity tolerance by supporting gill cell function during hyperosmotic stress. General significance: Involvement of tilapia GRAIL in the osmotic stress response suggests that GRAIL E3 ubiquitin ligases play a broader role in environmental stress responses, beyond their documented functions in adaptive immunity and development.
Fil: Fiol, Diego Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Biológicas; Argentina. Universidad Nacional de Mar del Plata; Argentina. University Of California At Davis; Estados Unidos
Fil: Sanmarti, Enio. University Of California At Davis; Estados Unidos
Fil: Lim, Andreana H.. University Of California At Davis; Estados Unidos
Fil: Kültz, Dietmar. University Of California At Davis; Estados Unidos
description Background: Tilapia (Oreochromis mossambicus) are euryhaline fishes capable of tolerating large salinity changes. In a previous study aimed to identify genes involved in osmotolerance, we isolated an mRNA sequence with similarity to GRAIL (Gene Related to Anergy In Lymphocytes), which is a critical regulator of adaptive immunity and development. Tilapia GRAIL contains a PA (protease associated) domain and a C3H2C3 RING finger domain indicative of E3 ubiquitin ligase activity. Scope of review: Western blots analysis was used to assess GRAIL expression pattern and responses to hyperosmotic stress. Immunohistochemistry was used to reveal the cellular localization of GRAIL in gill epithelium. Overexpression in HEK293 T-Rex cells was used to functionally characterize tilapia GRAIL. Salinity stress causes strong up-regulation of both mRNA and protein levels of tilapia GRAIL in gill epithelium. Tissue distribution of GRAIL protein is mainly confined to gill epithelium, which is the primary tissue responsible for osmoregulation of teleost fishes. Overexpression of tilapia GRAIL in HEK293 cells increases cell survival (cell viability) while decreases apoptosis during salinity challenge. Major conclusions: Our data indicate that tilapia GRAIL is a novel E3 ubiquitin ligase involved in osmotic stress signaling, which promotes environmental salinity tolerance by supporting gill cell function during hyperosmotic stress. General significance: Involvement of tilapia GRAIL in the osmotic stress response suggests that GRAIL E3 ubiquitin ligases play a broader role in environmental stress responses, beyond their documented functions in adaptive immunity and development.
publishDate 2011
dc.date.none.fl_str_mv 2011-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/13064
Fiol, Diego Fernando; Sanmarti, Enio; Lim, Andreana H.; Kültz, Dietmar; A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1810; 4; 4-2011; 439-445
0304-4165
url http://hdl.handle.net/11336/13064
identifier_str_mv Fiol, Diego Fernando; Sanmarti, Enio; Lim, Andreana H.; Kültz, Dietmar; A novel GRAIL E3 ubiquitin ligase promotes environmental salinity tolerance in euryhaline tilapia; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1810; 4; 4-2011; 439-445
0304-4165
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0304416510002552
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2010.11.005
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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