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Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway

The Arabidopsis SOS2 family of twenty-six protein kinases (CIPKs), their interacting activators, the SOS3 family of ten calcium-binding proteins (CBLs) and protein phosphatases type 2C (PP2C), function together in decoding calcium signals elicited by different environmental stimuli. Biochemical data...

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Autores principales: Sánchez-Barrena, María José, Martínez-Ripoll, Martín, Albert, Armando
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634423/
https://www.ncbi.nlm.nih.gov/pubmed/23481636
http://dx.doi.org/10.3390/ijms14035734
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author Sánchez-Barrena, María José
Martínez-Ripoll, Martín
Albert, Armando
author_facet Sánchez-Barrena, María José
Martínez-Ripoll, Martín
Albert, Armando
author_sort Sánchez-Barrena, María José
collection PubMed
description The Arabidopsis SOS2 family of twenty-six protein kinases (CIPKs), their interacting activators, the SOS3 family of ten calcium-binding proteins (CBLs) and protein phosphatases type 2C (PP2C), function together in decoding calcium signals elicited by different environmental stimuli. Biochemical data suggest that stable CBL-CIPK or CIPK-PP2C complexes may be regulating the activity of various substrates controlling ion homeostasis. The available structural information provides a general regulatory mechanism in which calcium perception by CBLs and kinase activation is coupled. The structural basis of this molecular mechanism and the specificity of the network is reviewed and discussed in detail.
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spelling pubmed-36344232013-05-02 Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway Sánchez-Barrena, María José Martínez-Ripoll, Martín Albert, Armando Int J Mol Sci Review The Arabidopsis SOS2 family of twenty-six protein kinases (CIPKs), their interacting activators, the SOS3 family of ten calcium-binding proteins (CBLs) and protein phosphatases type 2C (PP2C), function together in decoding calcium signals elicited by different environmental stimuli. Biochemical data suggest that stable CBL-CIPK or CIPK-PP2C complexes may be regulating the activity of various substrates controlling ion homeostasis. The available structural information provides a general regulatory mechanism in which calcium perception by CBLs and kinase activation is coupled. The structural basis of this molecular mechanism and the specificity of the network is reviewed and discussed in detail. Molecular Diversity Preservation International (MDPI) 2013-03-12 /pmc/articles/PMC3634423/ /pubmed/23481636 http://dx.doi.org/10.3390/ijms14035734 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0 This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Sánchez-Barrena, María José
Martínez-Ripoll, Martín
Albert, Armando
Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title_full Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title_fullStr Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title_full_unstemmed Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title_short Structural Biology of a Major Signaling Network that Regulates Plant Abiotic Stress: The CBL-CIPK Mediated Pathway
title_sort structural biology of a major signaling network that regulates plant abiotic stress: the cbl-cipk mediated pathway
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3634423/
https://www.ncbi.nlm.nih.gov/pubmed/23481636
http://dx.doi.org/10.3390/ijms14035734
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