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REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement

Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 protein...

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Autores principales: Perraki, Artemis, Gronnier, Julien, Gouguet, Paul, Boudsocq, Marie, Deroubaix, Anne-Flore, Simon, Vincent, German-Retana, Sylvie, Legrand, Anthony, Habenstein, Birgit, Zipfel, Cyril, Bayer, Emmanuelle, Mongrand, Sébastien, Germain, Véronique
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6258466/
https://www.ncbi.nlm.nih.gov/pubmed/30419072
http://dx.doi.org/10.1371/journal.ppat.1007378
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author Perraki, Artemis
Gronnier, Julien
Gouguet, Paul
Boudsocq, Marie
Deroubaix, Anne-Flore
Simon, Vincent
German-Retana, Sylvie
Legrand, Anthony
Habenstein, Birgit
Zipfel, Cyril
Bayer, Emmanuelle
Mongrand, Sébastien
Germain, Véronique
author_facet Perraki, Artemis
Gronnier, Julien
Gouguet, Paul
Boudsocq, Marie
Deroubaix, Anne-Flore
Simon, Vincent
German-Retana, Sylvie
Legrand, Anthony
Habenstein, Birgit
Zipfel, Cyril
Bayer, Emmanuelle
Mongrand, Sébastien
Germain, Véronique
author_sort Perraki, Artemis
collection PubMed
description Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3's phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses.
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spelling pubmed-62584662018-12-06 REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement Perraki, Artemis Gronnier, Julien Gouguet, Paul Boudsocq, Marie Deroubaix, Anne-Flore Simon, Vincent German-Retana, Sylvie Legrand, Anthony Habenstein, Birgit Zipfel, Cyril Bayer, Emmanuelle Mongrand, Sébastien Germain, Véronique PLoS Pathog Research Article Plants respond to pathogens through dynamic regulation of plasma membrane-bound signaling pathways. To date, how the plant plasma membrane is involved in responses to viruses is mostly unknown. Here, we show that plant cells sense the Potato virus X (PVX) COAT PROTEIN and TRIPLE GENE BLOCK 1 proteins and subsequently trigger the activation of a membrane-bound calcium-dependent kinase. We show that the Arabidopsis thaliana CALCIUM-DEPENDENT PROTEIN KINASE 3-interacts with group 1 REMORINs in vivo, phosphorylates the intrinsically disordered N-terminal domain of the Group 1 REMORIN REM1.3, and restricts PVX cell-to-cell movement. REM1.3's phospho-status defines its plasma membrane nanodomain organization and is crucial for REM1.3-dependent restriction of PVX cell-to-cell movement by regulation of callose deposition at plasmodesmata. This study unveils plasma membrane nanodomain-associated molecular events underlying the plant immune response to viruses. Public Library of Science 2018-11-12 /pmc/articles/PMC6258466/ /pubmed/30419072 http://dx.doi.org/10.1371/journal.ppat.1007378 Text en © 2018 Perraki et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Perraki, Artemis
Gronnier, Julien
Gouguet, Paul
Boudsocq, Marie
Deroubaix, Anne-Flore
Simon, Vincent
German-Retana, Sylvie
Legrand, Anthony
Habenstein, Birgit
Zipfel, Cyril
Bayer, Emmanuelle
Mongrand, Sébastien
Germain, Véronique
REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title_full REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title_fullStr REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title_full_unstemmed REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title_short REM1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting PVX cell-to-cell movement
title_sort rem1.3's phospho-status defines its plasma membrane nanodomain organization and activity in restricting pvx cell-to-cell movement
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6258466/
https://www.ncbi.nlm.nih.gov/pubmed/30419072
http://dx.doi.org/10.1371/journal.ppat.1007378
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