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A calmodulin‐like protein regulates plasmodesmal closure during bacterial immune responses
Author(s) -
Xu Bo,
Cheval Cécilia,
Laohavisit Anuphon,
Hocking Bradleigh,
Chiasson David,
Olsson Tjelvar S. G.,
Shirasu Ken,
Faulkner Christine,
Gilliham Matthew
Publication year - 2017
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.14599
Subject(s) - plasmodesma , biology , callose , microbiology and biotechnology , flagellin , calmodulin , botany , biochemistry , receptor , cell wall , cytoplasm , enzyme
Summary Plants sense microbial signatures via activation of pattern recognition receptors ( PPR s), 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 ( CML 41). CML 41 is transcriptionally upregulated by flg22 and facilitates rapid callose deposition at plasmodesmata following flg22 treatment. CML 41 acts independently of other defence responses triggered by flg22 perception and reduces bacterial infection. We propose that CML 41 enables Ca 2+ ‐signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae .