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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/13064
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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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1846082972559605760 |
score |
13.22299 |