PKA isoforms coordinate mRNA fate during nutrient starvation
- Autores
- Tudisca, Vanesa Romina; Simpson, Clare; Castelli, Lydia; Lui, Jennifer; Hoyle, Nathaniel; Moreno, Silvia Margarita; Ashe, Mark; Portela, Paula
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- A variety of stress conditions induce mRNA and protein aggregation into mRNA silencing foci, but the signalling pathways mediating these responses are still elusive. Previously we demonstrated that PKA catalytic isoforms Tpk2 and Tpk3 localise with processing and stress bodies in Saccharomyces cerevisiae. Here, we show that Tpk2 and Tpk3 are associated with translation initiation factors Pab1 and Rps3 in exponentially growing cells. Glucose starvation promotes the loss of interaction between Tpk and initiation factors followed by their accumulation into processing bodies. Analysis of mutants of the individual PKA isoform genes has revealed that the TPK3 or TPK2 deletion affects the capacity of the cells to form granules and arrest translation properly in response to glucose starvation or stationary phase. Moreover, we demonstrate that PKA controls Rpg1 and eIF4G1 protein abundance, possibly controlling cap-dependent translation. Taken together,our data suggest that the PKA pathway coordinates multiple stages in the fate of mRNAs in association with nutritional environment and growth status of the cell. © 2012.
Fil: Tudisca, Vanesa Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Simpson, Clare. University of Manchester; Reino Unido
Fil: Castelli, Lydia. University of Manchester; Reino Unido
Fil: Lui, Jennifer. University of Manchester; Reino Unido
Fil: Hoyle, Nathaniel. University of Manchester; Reino Unido
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina
Fil: Ashe, Mark. University of Manchester; Reino Unido
Fil: Portela, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina - Materia
-
PKA
SACCHAROMYCES CEREVISIAE
TRANSLATION - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/66665
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PKA isoforms coordinate mRNA fate during nutrient starvationTudisca, Vanesa RominaSimpson, ClareCastelli, LydiaLui, JenniferHoyle, NathanielMoreno, Silvia MargaritaAshe, MarkPortela, PaulaPKASACCHAROMYCES CEREVISIAETRANSLATIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A variety of stress conditions induce mRNA and protein aggregation into mRNA silencing foci, but the signalling pathways mediating these responses are still elusive. Previously we demonstrated that PKA catalytic isoforms Tpk2 and Tpk3 localise with processing and stress bodies in Saccharomyces cerevisiae. Here, we show that Tpk2 and Tpk3 are associated with translation initiation factors Pab1 and Rps3 in exponentially growing cells. Glucose starvation promotes the loss of interaction between Tpk and initiation factors followed by their accumulation into processing bodies. Analysis of mutants of the individual PKA isoform genes has revealed that the TPK3 or TPK2 deletion affects the capacity of the cells to form granules and arrest translation properly in response to glucose starvation or stationary phase. Moreover, we demonstrate that PKA controls Rpg1 and eIF4G1 protein abundance, possibly controlling cap-dependent translation. Taken together,our data suggest that the PKA pathway coordinates multiple stages in the fate of mRNAs in association with nutritional environment and growth status of the cell. © 2012.Fil: Tudisca, Vanesa Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Simpson, Clare. University of Manchester; Reino UnidoFil: Castelli, Lydia. University of Manchester; Reino UnidoFil: Lui, Jennifer. University of Manchester; Reino UnidoFil: Hoyle, Nathaniel. University of Manchester; Reino UnidoFil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaFil: Ashe, Mark. University of Manchester; Reino UnidoFil: Portela, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; ArgentinaCompany of Biologists2012-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/66665Tudisca, Vanesa Romina; Simpson, Clare; Castelli, Lydia; Lui, Jennifer; Hoyle, Nathaniel; et al.; PKA isoforms coordinate mRNA fate during nutrient starvation; Company of Biologists; Journal of Cell Science; 125; 21; 8-2012; 5221-52320021-9533CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.111534info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/125/21/5221info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:37:32Zoai:ri.conicet.gov.ar:11336/66665instacron: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:34982025-09-29 10:37:32.62CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
PKA isoforms coordinate mRNA fate during nutrient starvation |
title |
PKA isoforms coordinate mRNA fate during nutrient starvation |
spellingShingle |
PKA isoforms coordinate mRNA fate during nutrient starvation Tudisca, Vanesa Romina PKA SACCHAROMYCES CEREVISIAE TRANSLATION |
title_short |
PKA isoforms coordinate mRNA fate during nutrient starvation |
title_full |
PKA isoforms coordinate mRNA fate during nutrient starvation |
title_fullStr |
PKA isoforms coordinate mRNA fate during nutrient starvation |
title_full_unstemmed |
PKA isoforms coordinate mRNA fate during nutrient starvation |
title_sort |
PKA isoforms coordinate mRNA fate during nutrient starvation |
dc.creator.none.fl_str_mv |
Tudisca, Vanesa Romina Simpson, Clare Castelli, Lydia Lui, Jennifer Hoyle, Nathaniel Moreno, Silvia Margarita Ashe, Mark Portela, Paula |
author |
Tudisca, Vanesa Romina |
author_facet |
Tudisca, Vanesa Romina Simpson, Clare Castelli, Lydia Lui, Jennifer Hoyle, Nathaniel Moreno, Silvia Margarita Ashe, Mark Portela, Paula |
author_role |
author |
author2 |
Simpson, Clare Castelli, Lydia Lui, Jennifer Hoyle, Nathaniel Moreno, Silvia Margarita Ashe, Mark Portela, Paula |
author2_role |
author author author author author author author |
dc.subject.none.fl_str_mv |
PKA SACCHAROMYCES CEREVISIAE TRANSLATION |
topic |
PKA SACCHAROMYCES CEREVISIAE TRANSLATION |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
A variety of stress conditions induce mRNA and protein aggregation into mRNA silencing foci, but the signalling pathways mediating these responses are still elusive. Previously we demonstrated that PKA catalytic isoforms Tpk2 and Tpk3 localise with processing and stress bodies in Saccharomyces cerevisiae. Here, we show that Tpk2 and Tpk3 are associated with translation initiation factors Pab1 and Rps3 in exponentially growing cells. Glucose starvation promotes the loss of interaction between Tpk and initiation factors followed by their accumulation into processing bodies. Analysis of mutants of the individual PKA isoform genes has revealed that the TPK3 or TPK2 deletion affects the capacity of the cells to form granules and arrest translation properly in response to glucose starvation or stationary phase. Moreover, we demonstrate that PKA controls Rpg1 and eIF4G1 protein abundance, possibly controlling cap-dependent translation. Taken together,our data suggest that the PKA pathway coordinates multiple stages in the fate of mRNAs in association with nutritional environment and growth status of the cell. © 2012. Fil: Tudisca, Vanesa Romina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina Fil: Simpson, Clare. University of Manchester; Reino Unido Fil: Castelli, Lydia. University of Manchester; Reino Unido Fil: Lui, Jennifer. University of Manchester; Reino Unido Fil: Hoyle, Nathaniel. University of Manchester; Reino Unido Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina Fil: Ashe, Mark. University of Manchester; Reino Unido Fil: Portela, Paula. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina |
description |
A variety of stress conditions induce mRNA and protein aggregation into mRNA silencing foci, but the signalling pathways mediating these responses are still elusive. Previously we demonstrated that PKA catalytic isoforms Tpk2 and Tpk3 localise with processing and stress bodies in Saccharomyces cerevisiae. Here, we show that Tpk2 and Tpk3 are associated with translation initiation factors Pab1 and Rps3 in exponentially growing cells. Glucose starvation promotes the loss of interaction between Tpk and initiation factors followed by their accumulation into processing bodies. Analysis of mutants of the individual PKA isoform genes has revealed that the TPK3 or TPK2 deletion affects the capacity of the cells to form granules and arrest translation properly in response to glucose starvation or stationary phase. Moreover, we demonstrate that PKA controls Rpg1 and eIF4G1 protein abundance, possibly controlling cap-dependent translation. Taken together,our data suggest that the PKA pathway coordinates multiple stages in the fate of mRNAs in association with nutritional environment and growth status of the cell. © 2012. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-08 |
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/11336/66665 Tudisca, Vanesa Romina; Simpson, Clare; Castelli, Lydia; Lui, Jennifer; Hoyle, Nathaniel; et al.; PKA isoforms coordinate mRNA fate during nutrient starvation; Company of Biologists; Journal of Cell Science; 125; 21; 8-2012; 5221-5232 0021-9533 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/66665 |
identifier_str_mv |
Tudisca, Vanesa Romina; Simpson, Clare; Castelli, Lydia; Lui, Jennifer; Hoyle, Nathaniel; et al.; PKA isoforms coordinate mRNA fate during nutrient starvation; Company of Biologists; Journal of Cell Science; 125; 21; 8-2012; 5221-5232 0021-9533 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1242/jcs.111534 info:eu-repo/semantics/altIdentifier/url/http://jcs.biologists.org/content/125/21/5221 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Company of Biologists |
publisher.none.fl_str_mv |
Company of Biologists |
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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13.070432 |