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Type: Journal article
Title: A calmodulin-like protein regulates plasmodesmal closure during bacterial immune responses
Author: Xu, B.
Cheval, C.
Laohavisit, A.
Hocking, B.
Chiasson, D.
Olsson, T.
Shirasu, K.
Faulkner, C.
Gilliham, M.
Citation: New Phytologist, 2017; 215(1):77-84
Publisher: New Phytologist Trust
Issue Date: 2017
ISSN: 0028-646X
Statement of
Bo Xu, Cecilia Cheval, Anuphon Laohavisit, Bradleigh Hocking, David Chiasson, Tjelvar S. G. Olsson, Ken Shirasu, Christine Faulkner and Matthew Gilliham
Abstract: 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 Ca2+ -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 Ca2+ -signalling specificity during bacterial pathogen attack and is required for a complete defence response against Pseudomonas syringae.
Keywords: At3g50770
biotic stress
cell-to-cell communication
electrophoresis mobility shift
maltose-binding protein
pathogen-associated molecular pattern (PAMP)
Rights: © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
DOI: 10.1111/nph.14599
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