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Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in glycolysis and shown, particularly in animal cells, to play additional roles in several unrelated non-metabolic processes such as control of gene expression and apoptosis. This functional versatility is regulated, in...

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Autores principales: Zaffagnini, Mirko, Fermani, Simona, Costa, Alex, Lemaire, Stéphane D., Trost, Paolo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3824636/
https://www.ncbi.nlm.nih.gov/pubmed/24282406
http://dx.doi.org/10.3389/fpls.2013.00450
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author Zaffagnini, Mirko
Fermani, Simona
Costa, Alex
Lemaire, Stéphane D.
Trost, Paolo
author_facet Zaffagnini, Mirko
Fermani, Simona
Costa, Alex
Lemaire, Stéphane D.
Trost, Paolo
author_sort Zaffagnini, Mirko
collection PubMed
description Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in glycolysis and shown, particularly in animal cells, to play additional roles in several unrelated non-metabolic processes such as control of gene expression and apoptosis. This functional versatility is regulated, in part at least, by redox post-translational modifications that alter GAPDH catalytic activity and influence the subcellular localization of the enzyme. In spite of the well established moonlighting (multifunctional) properties of animal GAPDH, little is known about non-metabolic roles of GAPDH in plants. Plant cells contain several GAPDH isoforms with different catalytic and regulatory properties, located both in the cytoplasm and in plastids, and participating in glycolysis and the Calvin-Benson cycle. A general feature of all GAPDH proteins is the presence of an acidic catalytic cysteine in the active site that is overly sensitive to oxidative modifications, including glutathionylation and S-nitrosylation. In Arabidopsis, oxidatively modified cytoplasmic GAPDH has been successfully used as a tool to investigate the role of reduced glutathione, thioredoxins and glutaredoxins in the control of different types of redox post-translational modifications. Oxidative modifications inhibit GAPDH activity, but might enable additional functions in plant cells. Mounting evidence support the concept that plant cytoplasmic GAPDH may fulfill alternative, non-metabolic functions that are triggered by redox post-translational modifications of the protein under stress conditions. The aim of this review is to detail the molecular mechanisms underlying the redox regulation of plant cytoplasmic GAPDH in the light of its crystal structure, and to provide a brief inventory of the well known redox-dependent multi-facetted properties of animal GAPDH, together with the emerging roles of oxidatively modified GAPDH in stress signaling pathways in plants.
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spelling pubmed-38246362013-11-26 Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties Zaffagnini, Mirko Fermani, Simona Costa, Alex Lemaire, Stéphane D. Trost, Paolo Front Plant Sci Plant Science Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a ubiquitous enzyme involved in glycolysis and shown, particularly in animal cells, to play additional roles in several unrelated non-metabolic processes such as control of gene expression and apoptosis. This functional versatility is regulated, in part at least, by redox post-translational modifications that alter GAPDH catalytic activity and influence the subcellular localization of the enzyme. In spite of the well established moonlighting (multifunctional) properties of animal GAPDH, little is known about non-metabolic roles of GAPDH in plants. Plant cells contain several GAPDH isoforms with different catalytic and regulatory properties, located both in the cytoplasm and in plastids, and participating in glycolysis and the Calvin-Benson cycle. A general feature of all GAPDH proteins is the presence of an acidic catalytic cysteine in the active site that is overly sensitive to oxidative modifications, including glutathionylation and S-nitrosylation. In Arabidopsis, oxidatively modified cytoplasmic GAPDH has been successfully used as a tool to investigate the role of reduced glutathione, thioredoxins and glutaredoxins in the control of different types of redox post-translational modifications. Oxidative modifications inhibit GAPDH activity, but might enable additional functions in plant cells. Mounting evidence support the concept that plant cytoplasmic GAPDH may fulfill alternative, non-metabolic functions that are triggered by redox post-translational modifications of the protein under stress conditions. The aim of this review is to detail the molecular mechanisms underlying the redox regulation of plant cytoplasmic GAPDH in the light of its crystal structure, and to provide a brief inventory of the well known redox-dependent multi-facetted properties of animal GAPDH, together with the emerging roles of oxidatively modified GAPDH in stress signaling pathways in plants. Frontiers Media S.A. 2013-11-12 /pmc/articles/PMC3824636/ /pubmed/24282406 http://dx.doi.org/10.3389/fpls.2013.00450 Text en Copyright © 2013 Zaffagnini, Fermani, Costa, Lemaire and Trost. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Zaffagnini, Mirko
Fermani, Simona
Costa, Alex
Lemaire, Stéphane D.
Trost, Paolo
Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title_full Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title_fullStr Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title_full_unstemmed Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title_short Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
title_sort plant cytoplasmic gapdh: redox post-translational modifications and moonlighting properties
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3824636/
https://www.ncbi.nlm.nih.gov/pubmed/24282406
http://dx.doi.org/10.3389/fpls.2013.00450
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