Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae

Autores
Galello, Fiorella Ariadna; Moreno, Silvia Margarita; Rossi, Silvia Graciela
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
cAMP-dependent protein kinase mediates many extracellular signals in eukaryotes. The compartmentalization of PKA is an important level of control of the specificity of signal transduction mediated by cAMP. Unlike mammalian PKA for which proof insights in the mechanism that controls its localization through anchoring proteins (AKAPs) has been obtained, in the case of Saccharomyces cerevisiae PKA there was little information available. In this work, we present results that demonstrate the isolation and identification of yeast PKA regulatory subunit (Bcy1) associated proteins using a MS-based proteomic analysis and a bioinformatic approach. The verification of some of these interactions was assessed by immunoprecipitation, pull down and co-localization by subcellular fractionation. The key role of positively charged residues present in the interaction domain of the identified proteins was demonstrated. The defined interaction domain has therefore different molecular characteristics than conventional AKAP domains. Finally we assess initial experiments to visualize the physiological relevance of the interaction of both Ira2 and Hsp60 with Bcy1. Bcy1 interacts with Ira2 tethering PKA to the Ras complex and Hsp60 chaperone localizes PKA to mitochondria and has a role in the kinase stability.
Fil: Galello, Fiorella Ariadna. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Rossi, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Materia
Pka
Bcy1
Saccharomyces Cerevisiae
Anchoring Proteins
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:11336/31999
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/31999
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiaeGalello, Fiorella AriadnaMoreno, Silvia MargaritaRossi, Silvia GracielaPkaBcy1Saccharomyces CerevisiaeAnchoring Proteinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1cAMP-dependent protein kinase mediates many extracellular signals in eukaryotes. The compartmentalization of PKA is an important level of control of the specificity of signal transduction mediated by cAMP. Unlike mammalian PKA for which proof insights in the mechanism that controls its localization through anchoring proteins (AKAPs) has been obtained, in the case of Saccharomyces cerevisiae PKA there was little information available. In this work, we present results that demonstrate the isolation and identification of yeast PKA regulatory subunit (Bcy1) associated proteins using a MS-based proteomic analysis and a bioinformatic approach. The verification of some of these interactions was assessed by immunoprecipitation, pull down and co-localization by subcellular fractionation. The key role of positively charged residues present in the interaction domain of the identified proteins was demonstrated. The defined interaction domain has therefore different molecular characteristics than conventional AKAP domains. Finally we assess initial experiments to visualize the physiological relevance of the interaction of both Ira2 and Hsp60 with Bcy1. Bcy1 interacts with Ira2 tethering PKA to the Ras complex and Hsp60 chaperone localizes PKA to mitochondria and has a role in the kinase stability.Fil: Galello, Fiorella Ariadna. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Rossi, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaElsevier Science2014-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31999Rossi, Silvia Graciela; Moreno, Silvia Margarita; Galello, Fiorella Ariadna; Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae; Elsevier Science; Journal Of Proteomics; 109; 7-2014; 261-2751874-3919CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jprot.2014.07.008info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1874391914003601info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:50Zoai:ri.conicet.gov.ar:11336/31999instacron: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:34982025-09-03 09:59:50.723CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
title Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
spellingShingle Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
Galello, Fiorella Ariadna
Pka
Bcy1
Saccharomyces Cerevisiae
Anchoring Proteins
title_short Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
title_full Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
title_fullStr Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
title_full_unstemmed Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
title_sort Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae
dc.creator.none.fl_str_mv Galello, Fiorella Ariadna
Moreno, Silvia Margarita
Rossi, Silvia Graciela
author Galello, Fiorella Ariadna
author_facet Galello, Fiorella Ariadna
Moreno, Silvia Margarita
Rossi, Silvia Graciela
author_role author
author2 Moreno, Silvia Margarita
Rossi, Silvia Graciela
author2_role author
author
dc.subject.none.fl_str_mv Pka
Bcy1
Saccharomyces Cerevisiae
Anchoring Proteins
topic Pka
Bcy1
Saccharomyces Cerevisiae
Anchoring Proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv cAMP-dependent protein kinase mediates many extracellular signals in eukaryotes. The compartmentalization of PKA is an important level of control of the specificity of signal transduction mediated by cAMP. Unlike mammalian PKA for which proof insights in the mechanism that controls its localization through anchoring proteins (AKAPs) has been obtained, in the case of Saccharomyces cerevisiae PKA there was little information available. In this work, we present results that demonstrate the isolation and identification of yeast PKA regulatory subunit (Bcy1) associated proteins using a MS-based proteomic analysis and a bioinformatic approach. The verification of some of these interactions was assessed by immunoprecipitation, pull down and co-localization by subcellular fractionation. The key role of positively charged residues present in the interaction domain of the identified proteins was demonstrated. The defined interaction domain has therefore different molecular characteristics than conventional AKAP domains. Finally we assess initial experiments to visualize the physiological relevance of the interaction of both Ira2 and Hsp60 with Bcy1. Bcy1 interacts with Ira2 tethering PKA to the Ras complex and Hsp60 chaperone localizes PKA to mitochondria and has a role in the kinase stability.
Fil: Galello, Fiorella Ariadna. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Moreno, Silvia Margarita. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Rossi, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
description cAMP-dependent protein kinase mediates many extracellular signals in eukaryotes. The compartmentalization of PKA is an important level of control of the specificity of signal transduction mediated by cAMP. Unlike mammalian PKA for which proof insights in the mechanism that controls its localization through anchoring proteins (AKAPs) has been obtained, in the case of Saccharomyces cerevisiae PKA there was little information available. In this work, we present results that demonstrate the isolation and identification of yeast PKA regulatory subunit (Bcy1) associated proteins using a MS-based proteomic analysis and a bioinformatic approach. The verification of some of these interactions was assessed by immunoprecipitation, pull down and co-localization by subcellular fractionation. The key role of positively charged residues present in the interaction domain of the identified proteins was demonstrated. The defined interaction domain has therefore different molecular characteristics than conventional AKAP domains. Finally we assess initial experiments to visualize the physiological relevance of the interaction of both Ira2 and Hsp60 with Bcy1. Bcy1 interacts with Ira2 tethering PKA to the Ras complex and Hsp60 chaperone localizes PKA to mitochondria and has a role in the kinase stability.
publishDate 2014
dc.date.none.fl_str_mv 2014-07
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/11336/31999
Rossi, Silvia Graciela; Moreno, Silvia Margarita; Galello, Fiorella Ariadna; Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae; Elsevier Science; Journal Of Proteomics; 109; 7-2014; 261-275
1874-3919
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31999
identifier_str_mv Rossi, Silvia Graciela; Moreno, Silvia Margarita; Galello, Fiorella Ariadna; Interacting proteins of protein kinase A regulatory subunit in Saccharomyces cerevisiae; Elsevier Science; Journal Of Proteomics; 109; 7-2014; 261-275
1874-3919
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jprot.2014.07.008
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1874391914003601
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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score 13.13397

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