Plant PP2A: A Versatile Enzyme with Key Physiological Functions

Autores
Cortelezzi, Juan Ignacio; Zubillaga, Martina; Scardino, Victoria Raquel; Muñiz García, María Noelia; Capiati, Daniela Andrea
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The Arabidopsis thaliana genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts.
Fil: Cortelezzi, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Zubillaga, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Scardino, Victoria Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Muñiz García, María Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Capiati, Daniela Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Materia
ABIOTIC STRESS
BIOTIC STRESS
DEVELOPMENT
PHOSPHATASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/279973
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Plant PP2A: A Versatile Enzyme with Key Physiological FunctionsCortelezzi, Juan IgnacioZubillaga, MartinaScardino, Victoria RaquelMuñiz García, María NoeliaCapiati, Daniela AndreaABIOTIC STRESSBIOTIC STRESSDEVELOPMENTPHOSPHATASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The Arabidopsis thaliana genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts.Fil: Cortelezzi, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Zubillaga, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Scardino, Victoria Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Muñiz García, María Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Capiati, Daniela Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaMultidisciplinary Digital Publishing Institute2025-03-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/279973Cortelezzi, Juan Ignacio; Zubillaga, Martina; Scardino, Victoria Raquel; Muñiz García, María Noelia; Capiati, Daniela Andrea; Plant PP2A: A Versatile Enzyme with Key Physiological Functions; Multidisciplinary Digital Publishing Institute; Kinases and Phosphatases; 3; 1; 3-3-2025; 1-122813-3757CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2813-3757/3/1/5info:eu-repo/semantics/altIdentifier/doi/ 10.3390/kinasesphosphatases3010005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-06T13:46:46Zoai:ri.conicet.gov.ar:11336/279973instacron: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:34982026-02-06 13:46:46.315CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Plant PP2A: A Versatile Enzyme with Key Physiological Functions
title Plant PP2A: A Versatile Enzyme with Key Physiological Functions
spellingShingle Plant PP2A: A Versatile Enzyme with Key Physiological Functions
Cortelezzi, Juan Ignacio
ABIOTIC STRESS
BIOTIC STRESS
DEVELOPMENT
PHOSPHATASE
title_short Plant PP2A: A Versatile Enzyme with Key Physiological Functions
title_full Plant PP2A: A Versatile Enzyme with Key Physiological Functions
title_fullStr Plant PP2A: A Versatile Enzyme with Key Physiological Functions
title_full_unstemmed Plant PP2A: A Versatile Enzyme with Key Physiological Functions
title_sort Plant PP2A: A Versatile Enzyme with Key Physiological Functions
dc.creator.none.fl_str_mv Cortelezzi, Juan Ignacio
Zubillaga, Martina
Scardino, Victoria Raquel
Muñiz García, María Noelia
Capiati, Daniela Andrea
author Cortelezzi, Juan Ignacio
author_facet Cortelezzi, Juan Ignacio
Zubillaga, Martina
Scardino, Victoria Raquel
Muñiz García, María Noelia
Capiati, Daniela Andrea
author_role author
author2 Zubillaga, Martina
Scardino, Victoria Raquel
Muñiz García, María Noelia
Capiati, Daniela Andrea
author2_role author
author
author
author
dc.subject.none.fl_str_mv ABIOTIC STRESS
BIOTIC STRESS
DEVELOPMENT
PHOSPHATASE
topic ABIOTIC STRESS
BIOTIC STRESS
DEVELOPMENT
PHOSPHATASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The Arabidopsis thaliana genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts.
Fil: Cortelezzi, Juan Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Zubillaga, Martina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Scardino, Victoria Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Muñiz García, María Noelia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Capiati, Daniela Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
description Protein phosphatase 2A (PP2A) is a highly conserved heterotrimeric enzyme complex present in all eukaryotic cells, consisting of a scaffolding A subunit, a catalytic C subunit, and a regulatory B subunit. The A and C subunits form the core enzyme, which interacts with the B subunit to determine the substrate specificity, subcellular localization, and enzymatic activity of the holoenzyme. The Arabidopsis thaliana genome encodes five C subunits, three A subunits, and 17 B subunits, enabling the formation of diverse holoenzymes with extensive functional versatility. Genetic evidence highlights the essential role of PP2A in regulating various physiological processes in plants, including responses to abiotic and biotic stresses and developmental programs. Notably, PP2A can act as both a positive and negative regulator within the same pathway, while individual subunits often participate in multiple processes. This functional diversity arises from the structural flexibility of PP2A. This review examines the structural diversity of plant PP2A and its regulatory roles across diverse physiological contexts.
publishDate 2025
dc.date.none.fl_str_mv 2025-03-03
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/11336/279973
Cortelezzi, Juan Ignacio; Zubillaga, Martina; Scardino, Victoria Raquel; Muñiz García, María Noelia; Capiati, Daniela Andrea; Plant PP2A: A Versatile Enzyme with Key Physiological Functions; Multidisciplinary Digital Publishing Institute; Kinases and Phosphatases; 3; 1; 3-3-2025; 1-12
2813-3757
CONICET Digital
CONICET
url http://hdl.handle.net/11336/279973
identifier_str_mv Cortelezzi, Juan Ignacio; Zubillaga, Martina; Scardino, Victoria Raquel; Muñiz García, María Noelia; Capiati, Daniela Andrea; Plant PP2A: A Versatile Enzyme with Key Physiological Functions; Multidisciplinary Digital Publishing Institute; Kinases and Phosphatases; 3; 1; 3-3-2025; 1-12
2813-3757
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2813-3757/3/1/5
info:eu-repo/semantics/altIdentifier/doi/ 10.3390/kinasesphosphatases3010005
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
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 12.595271

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