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Regulation of plant immune receptors by ubiquitination

From pathogen perception and the activation of signal transduction cascades to the deployment of defense responses, protein ubiquitination plays a key role in the modulation of plant immunity. Ubiquitination is mediated by three enzymes, of which the E3 ubiquitin ligases, the substrate determinants,...

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Detalles Bibliográficos
Autores principales: Furlan, Giulia, Klinkenberg, Jörn, Trujillo, Marco
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3479402/
https://www.ncbi.nlm.nih.gov/pubmed/23109936
http://dx.doi.org/10.3389/fpls.2012.00238
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author Furlan, Giulia
Klinkenberg, Jörn
Trujillo, Marco
author_facet Furlan, Giulia
Klinkenberg, Jörn
Trujillo, Marco
author_sort Furlan, Giulia
collection PubMed
description From pathogen perception and the activation of signal transduction cascades to the deployment of defense responses, protein ubiquitination plays a key role in the modulation of plant immunity. Ubiquitination is mediated by three enzymes, of which the E3 ubiquitin ligases, the substrate determinants, have been the major focus of attention. Accumulating evidence suggests that ubiquitination modulates signaling mediated by pattern recognition receptors and is important for the accumulation of nucleotide-binding leucine-rich repeat type intracellular immune sensors. Recent studies also indicate that ubiquitination directs vesicle trafficking, a function that has been clearly established for immune signaling in animals. In this mini review, we discuss these and other recent advances and highlight important open questions.
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spelling pubmed-34794022012-10-29 Regulation of plant immune receptors by ubiquitination Furlan, Giulia Klinkenberg, Jörn Trujillo, Marco Front Plant Sci Plant Science From pathogen perception and the activation of signal transduction cascades to the deployment of defense responses, protein ubiquitination plays a key role in the modulation of plant immunity. Ubiquitination is mediated by three enzymes, of which the E3 ubiquitin ligases, the substrate determinants, have been the major focus of attention. Accumulating evidence suggests that ubiquitination modulates signaling mediated by pattern recognition receptors and is important for the accumulation of nucleotide-binding leucine-rich repeat type intracellular immune sensors. Recent studies also indicate that ubiquitination directs vesicle trafficking, a function that has been clearly established for immune signaling in animals. In this mini review, we discuss these and other recent advances and highlight important open questions. Frontiers Media S.A. 2012-10-24 /pmc/articles/PMC3479402/ /pubmed/23109936 http://dx.doi.org/10.3389/fpls.2012.00238 Text en Copyright © Furlan, Klinkenberg and Trujillo. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) , which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.
spellingShingle Plant Science
Furlan, Giulia
Klinkenberg, Jörn
Trujillo, Marco
Regulation of plant immune receptors by ubiquitination
title Regulation of plant immune receptors by ubiquitination
title_full Regulation of plant immune receptors by ubiquitination
title_fullStr Regulation of plant immune receptors by ubiquitination
title_full_unstemmed Regulation of plant immune receptors by ubiquitination
title_short Regulation of plant immune receptors by ubiquitination
title_sort regulation of plant immune receptors by ubiquitination
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3479402/
https://www.ncbi.nlm.nih.gov/pubmed/23109936
http://dx.doi.org/10.3389/fpls.2012.00238
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