Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs

Abscisic acid (ABA) plays an essential function in plant physiology since it is required for biotic and abiotic stress responses as well as control of plant growth and development. A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of s...

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Autores: Santiago, Julia, Dupeux, Florine, Betz, Katja, Antoni, Regina, González-Guzmán, Miguel, Rodríguez, Lesia, Márquez, José Antonio, Rodríguez, Pedro L.
Tipo de recurso: artículo
Fecha de publicación:2012
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/48601
Acceso en línea:http://hdl.handle.net/10261/48601
Access Level:acceso abierto
Palabra clave:Protein phosphatase 2C
Abscisic-acid
Signal-transduction
Negative regulator
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spelling Structural insights into PYR/PYL/RCAR ABA receptors and PP2CsSantiago, JuliaDupeux, FlorineBetz, KatjaAntoni, ReginaGonzález-Guzmán, MiguelRodríguez, LesiaMárquez, José AntonioRodríguez, Pedro L.Protein phosphatase 2CAbscisic-acidSignal-transductionNegative regulatorAbscisic acid (ABA) plays an essential function in plant physiology since it is required for biotic and abiotic stress responses as well as control of plant growth and development. A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of specific protein phosphatases type-2C (PP2Cs) in an ABAdependent manner. The structural and functional mechanism by which ABA is perceived by these receptors and consequently leads to inhibition of the PP2Cs has been recently elucidated. The module PYR/PYL/RCARABA- PP2C offers an elegant and unprecedented mechanism to control phosphorylation signaling cascades in a ligand-dependent manner. The knowledge of their three-dimensional structures paves the way to the design of ABA agonists able to modulate the plant stress response.We are grateful to the European Synchrotron Radiation Facility (ESRF) and the EMBL for access to macromolecular crystallography beam lines. Work in the laboratory of Dr Rodriguez is supported by grant BIO2008- 00221 from Ministerio de Educación y Ciencia and Fondo Europeo de Desarrollo Regional and Consejo Superior de Investigaciones Científicas (fellowships to JS, RA and LR; Juan de la Cierva contract to MGG). Access to the high Throughput Crystallization facility of the Partnership for Structural Biology in Grenoble (PSB) (https://htxlab.embl.fr ) was supported by the European Community- Research Infrastructure Action PCUBE under the FP7 "Capacities" specific program.Peer reviewedElsevier201220122012info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/48601reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglésinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/486012026-05-22T06:33:51Z
dc.title.none.fl_str_mv Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
title Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
spellingShingle Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
Santiago, Julia
Protein phosphatase 2C
Abscisic-acid
Signal-transduction
Negative regulator
title_short Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
title_full Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
title_fullStr Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
title_full_unstemmed Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
title_sort Structural insights into PYR/PYL/RCAR ABA receptors and PP2Cs
dc.creator.none.fl_str_mv Santiago, Julia
Dupeux, Florine
Betz, Katja
Antoni, Regina
González-Guzmán, Miguel
Rodríguez, Lesia
Márquez, José Antonio
Rodríguez, Pedro L.
author Santiago, Julia
author_facet Santiago, Julia
Dupeux, Florine
Betz, Katja
Antoni, Regina
González-Guzmán, Miguel
Rodríguez, Lesia
Márquez, José Antonio
Rodríguez, Pedro L.
author_role author
author2 Dupeux, Florine
Betz, Katja
Antoni, Regina
González-Guzmán, Miguel
Rodríguez, Lesia
Márquez, José Antonio
Rodríguez, Pedro L.
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Protein phosphatase 2C
Abscisic-acid
Signal-transduction
Negative regulator
topic Protein phosphatase 2C
Abscisic-acid
Signal-transduction
Negative regulator
description Abscisic acid (ABA) plays an essential function in plant physiology since it is required for biotic and abiotic stress responses as well as control of plant growth and development. A new family of soluble ABA receptors, named PYR/PYL/RCAR, has emerged as ABA sensors able to inhibit the activity of specific protein phosphatases type-2C (PP2Cs) in an ABAdependent manner. The structural and functional mechanism by which ABA is perceived by these receptors and consequently leads to inhibition of the PP2Cs has been recently elucidated. The module PYR/PYL/RCARABA- PP2C offers an elegant and unprecedented mechanism to control phosphorylation signaling cascades in a ligand-dependent manner. The knowledge of their three-dimensional structures paves the way to the design of ABA agonists able to modulate the plant stress response.
publishDate 2012
dc.date.none.fl_str_mv 2012
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/48601
url http://hdl.handle.net/10261/48601
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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