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Author: Gronnier, Julien ; Bücherl, Christoph A ; Stransfeld, Lena ; Michard, Erwan ; Kadota, Yasuhiro ; Menke, Frank L H ; Derbyshire, Paul ; Scherzer, Sönke ; Feijó, José ; Wrzaczek, Michael ; Thor, Kathrin ; Dindas, Julian ; Charpentier, Myriam ; Hedrich, Rainer ; Kimura, Sachie ; Leitão, Nuno ; Huang, Shouguang ; Köster, Philipp ; Oldroyd, Giles E D ; Zipfel, Cyril ; DeFalco, Thomas A ; George, Jeoffrey ; Jiang, Shushu ; Roelfsema, M Rob G ; Hunter, Kerri ; MacLean, Daniel

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

24 Sep 2020·Nature

The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity

Article

Author: Gronnier, Julien ; Hunter, Kerri ; Stransfeld, Lena ; Michard, Erwan ; Kadota, Yasuhiro ; Menke, Frank L H ; Derbyshire, Paul ; Scherzer, Sönke ; Feijó, José ; Wrzaczek, Michael ; Thor, Kathrin ; Charpentier, Myriam ; Dindas, Julian ; Kimura, Sachie ; Huang, Shouguang ; Hedrich, Rainer ; Leitão, Nuno ; Köster, Philipp ; Oldroyd, Giles E D ; Zipfel, Cyril ; DeFalco, Thomas A ; Jiang, Shushu ; George, Jeoffrey ; Roelfsema, M Rob G ; MacLean, Daniel ; Bücherl, Christoph A

Perception of biotic and abiotic stresses often leads to stomatal closure in plants^1,2. Rapid influx of calcium ions (Ca²⁺) across the plasma membrane has an important role in this response, but the identity of the Ca²⁺ channels involved has remained elusive^3,4. Here we report that the Arabidopsis thaliana Ca²⁺-permeable channel OSCA1.3 controls stomatal closure during immune signalling. OSCA1.3 is rapidly phosphorylated upon perception of pathogen-associated molecular patterns (PAMPs). Biochemical and quantitative phosphoproteomics analyses reveal that the immune receptor-associated cytosolic kinase BIK1 interacts with and phosphorylates the N-terminal cytosolic loop of OSCA1.3 within minutes of treatment with the peptidic PAMP flg22, which is derived from bacterial flagellin. Genetic and electrophysiological data reveal that OSCA1.3 is permeable to Ca²⁺, and that BIK1-mediated phosphorylation on its N terminus increases this channel activity. Notably, OSCA1.3 and its phosphorylation by BIK1 are critical for stomatal closure during immune signalling, and OSCA1.3 does not regulate stomatal closure upon perception of abscisic acid-a plant hormone associated with abiotic stresses. This study thus identifies a plant Ca²⁺ channel and its activation mechanisms underlying stomatal closure during immune signalling, and suggests specificity in Ca²⁺ influx mechanisms in response to different stresses.

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