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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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2018
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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. |
format | Online Article Text |
id | pubmed-6258466 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
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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