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

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

  • Thor K The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Jiang S The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Michard E University of Maryland, Department of Cell Biology and Molecular Genetics, College Park, MD, USA.
  • George J The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Scherzer S Department of Molecular Plant Physiology and Biophysics, University of Würzburg, Würzburg, Germany.
  • Huang S Department of Molecular Plant Physiology and Biophysics, University of Würzburg, Würzburg, Germany.
  • Dindas J Institute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland.
  • Derbyshire P The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Leitão N Department of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.
  • DeFalco TA The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Köster P Institute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland.
  • Hunter K Organismal and Evolutionary Biology Research Programme, Viikki Plant Science Centre, VIPS, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
  • Kimura S Organismal and Evolutionary Biology Research Programme, Viikki Plant Science Centre, VIPS, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
  • Gronnier J The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Stransfeld L The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Kadota Y The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Bücherl CA The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Charpentier M Department of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.
  • Wrzaczek M Organismal and Evolutionary Biology Research Programme, Viikki Plant Science Centre, VIPS, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.
  • MacLean D The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Oldroyd GED Department of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, UK.
  • Menke FLH The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.
  • Roelfsema MRG Department of Molecular Plant Physiology and Biophysics, University of Würzburg, Würzburg, Germany.
  • Hedrich R Department of Molecular Plant Physiology and Biophysics, University of Würzburg, Würzburg, Germany.
  • Feijó J University of Maryland, Department of Cell Biology and Molecular Genetics, College Park, MD, USA.
  • Zipfel C The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK. cyril.zipfel@botinst.uzh.ch.
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  • 2020-08-27
Published in:
  • Nature. - 2020
Abscisic Acid
Arabidopsis
Arabidopsis Proteins
Calcium
Calcium Channels
Pathogen-Associated Molecular Pattern Molecules
Phosphorylation
Plant Immunity
Plant Stomata
Protein Binding
Protein-Serine-Threonine Kinases
Signal Transduction
English Perception of biotic and abiotic stresses often leads to stomatal closure in plants1,2. 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 elusive3,4. 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/169039
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