%0 Journal Article %1 RN990 %A Thor, K. %A Jiang, S. S. %A Michard, E. %A George, J. %A Scherzer, S. %A Huang, S. G. %A Dindas, J. %A Derbyshire, P. %A Leitao, N. %A DeFalco, T. A. %A Köster, P. %A Hunter, K. %A Kimura, S. %A Gronnier, J. %A Stransfeld, L. %A Kadota, Y. %A Bücherl, C. A. %A Charpentier, M. %A Wrzaczek, M. %A MacLean, D. %A Oldroyd, G. E. D. %A Menke, F. L. H. %A Roelfsema, M. R. G. %A Hedrich, R. %A Feijó, J. %A Zipfel, C. %D 2020 %J Nature %K myOwn nadph oxidase rbohd %N 7826 %P 569-+ %R 10.1038/s41586-020-2702-1 %T The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity %U /brokenurl#<Go to ISI>://WOS:000570130200001 %V 585 %X 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 Ca(2+)channels involved has remained elusive(3,4). Here we report that theArabidopsis thalianaCa(2+)-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 Ca(2+)channel and its activation mechanisms underlying stomatal closure during immune signalling, and suggests specificity in Ca(2+)influx mechanisms in response to different stresses. A study inArabidopsis thalianashows that the immune receptor-associated cytosolic kinase BIK1 phosphorylates OSCA1.3 and identifies OSCA1.3 as the pathogen-responsive Ca2+-permeable channel that regulates stomatal closure.

@article{RN990, abstract = {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 Ca(2+)channels involved has remained elusive(3,4). Here we report that theArabidopsis thalianaCa(2+)-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 Ca(2+)channel and its activation mechanisms underlying stomatal closure during immune signalling, and suggests specificity in Ca(2+)influx mechanisms in response to different stresses. A study inArabidopsis thalianashows that the immune receptor-associated cytosolic kinase BIK1 phosphorylates OSCA1.3 and identifies OSCA1.3 as the pathogen-responsive Ca2+-permeable channel that regulates stomatal closure.}, added-at = {2024-02-14T14:38:32.000+0100}, author = {Thor, K. and Jiang, S. S. and Michard, E. and George, J. and Scherzer, S. and Huang, S. G. and Dindas, J. and Derbyshire, P. and Leitao, N. and DeFalco, T. A. and Köster, P. and Hunter, K. and Kimura, S. and Gronnier, J. and Stransfeld, L. and Kadota, Y. and Bücherl, C. A. and Charpentier, M. and Wrzaczek, M. and MacLean, D. and Oldroyd, G. E. D. and Menke, F. L. H. and Roelfsema, M. R. G. and Hedrich, R. and Feijó, J. and Zipfel, C.}, biburl = {https://www.bibsonomy.org/bibtex/27f055958d6011b090fa2157c9238968c/rainerhedrich_2}, doi = {10.1038/s41586-020-2702-1}, interhash = {6ad8c3cb82638460f11ac9ae1bb94019}, intrahash = {7f055958d6011b090fa2157c9238968c}, issn = {0028-0836}, journal = {Nature}, keywords = {myOwn nadph oxidase rbohd}, note = {Ns9dw Times Cited:166 Cited References Count:61}, number = 7826, pages = {569-+}, timestamp = {2024-02-14T14:38:32.000+0100}, title = {The calcium-permeable channel OSCA1.3 regulates plant stomatal immunity}, type = {Journal Article}, url = {/brokenurl#<Go to ISI>://WOS:000570130200001}, volume = 585, year = 2020 }