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A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses
Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells. Plasmodesmal fl...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5488192/ https://www.ncbi.nlm.nih.gov/pubmed/28513846 http://dx.doi.org/10.1111/nph.14599 |
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author | Xu, Bo Cheval, Cécilia Laohavisit, Anuphon Hocking, Bradleigh Chiasson, David Olsson, Tjelvar S. G. Shirasu, Ken Faulkner, Christine Gilliham, Matthew |
author_facet | Xu, Bo Cheval, Cécilia Laohavisit, Anuphon Hocking, Bradleigh Chiasson, David Olsson, Tjelvar S. G. Shirasu, Ken Faulkner, Christine Gilliham, Matthew |
author_sort | Xu, Bo |
collection | PubMed |
description | Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells. Plasmodesmal flux is regulated by a variety of environmental cues but the downstream signalling pathways are poorly defined, especially the way in which calcium regulates plasmodesmal closure. Here, we identify that closure of plasmodesmata in response to bacterial flagellin, but not fungal chitin, is mediated by a plasmodesmal‐localized Ca(2+)‐binding protein Calmodulin‐like 41 (CML41). CML41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection. We propose that CML41 enables Ca(2+)‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae. |
format | Online Article Text |
id | pubmed-5488192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-54881922017-07-13 A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses Xu, Bo Cheval, Cécilia Laohavisit, Anuphon Hocking, Bradleigh Chiasson, David Olsson, Tjelvar S. G. Shirasu, Ken Faulkner, Christine Gilliham, Matthew New Phytol Research Plants sense microbial signatures via activation of pattern recognition receptors (PPRs), which trigger a range of cellular defences. One response is the closure of plasmodesmata, which reduces symplastic connectivity and the capacity for direct molecular exchange between host cells. Plasmodesmal flux is regulated by a variety of environmental cues but the downstream signalling pathways are poorly defined, especially the way in which calcium regulates plasmodesmal closure. Here, we identify that closure of plasmodesmata in response to bacterial flagellin, but not fungal chitin, is mediated by a plasmodesmal‐localized Ca(2+)‐binding protein Calmodulin‐like 41 (CML41). CML41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection. We propose that CML41 enables Ca(2+)‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae. John Wiley and Sons Inc. 2017-05-17 2017-07 /pmc/articles/PMC5488192/ /pubmed/28513846 http://dx.doi.org/10.1111/nph.14599 Text en © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Xu, Bo Cheval, Cécilia Laohavisit, Anuphon Hocking, Bradleigh Chiasson, David Olsson, Tjelvar S. G. Shirasu, Ken Faulkner, Christine Gilliham, Matthew A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title | A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title_full | A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title_fullStr | A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title_full_unstemmed | A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title_short | A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
title_sort | calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5488192/ https://www.ncbi.nlm.nih.gov/pubmed/28513846 http://dx.doi.org/10.1111/nph.14599 |
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