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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/66665

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network_name_str CONICET Digital (CONICET)
spelling 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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