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FRET kinase sensor development reveals SnRK2/OST1 activation by ABA but not by MeJA and high CO2 during stomatal closure.
Zhang, Li; Takahashi, Yohei; Hsu, Po-Kai; Kollist, Hannes; Merilo, Ebe; Krysan, Patrick J; Schroeder, Julian I.
Afiliación
  • Zhang L; Cell and Developmental Biology Section, Division of Biological Sciences, University of California, San Diego, San Diego, United States.
  • Takahashi Y; Cell and Developmental Biology Section, Division of Biological Sciences, University of California, San Diego, San Diego, United States.
  • Hsu PK; Cell and Developmental Biology Section, Division of Biological Sciences, University of California, San Diego, San Diego, United States.
  • Kollist H; Institute of Technology, University of Tartu, Tartu, Estonia.
  • Merilo E; Institute of Technology, University of Tartu, Tartu, Estonia.
  • Krysan PJ; Horticulture Department, University of Wisconsin-Madison, Madison, United States.
  • Schroeder JI; Cell and Developmental Biology Section, Division of Biological Sciences, University of California, San Diego, San Diego, United States.
Elife ; 92020 05 28.
Article en En | MEDLINE | ID: mdl-32463362
Sucrose-non-fermenting-1-related protein kinase-2s (SnRK2s) are critical for plant abiotic stress responses, including abscisic acid (ABA) signaling. Here, we develop a genetically encoded reporter for SnRK2 kinase activity. This sensor, named SNACS, shows an increase in the ratio of yellow to cyan fluorescence emission by OST1/SnRK2.6-mediated phosphorylation of a defined serine residue in SNACS. ABA rapidly increases FRET efficiency in N. benthamiana leaf cells and Arabidopsis guard cells. Interestingly, protein kinase inhibition decreases FRET efficiency in guard cells, providing direct experimental evidence that basal SnRK2 activity prevails in guard cells. Moreover, in contrast to ABA, the stomatal closing stimuli, elevated CO2 and MeJA, did not increase SNACS FRET ratios. These findings and gas exchange analyses of quintuple/sextuple ABA receptor mutants show that stomatal CO2 signaling requires basal ABA and SnRK2 signaling, but not SnRK2 activation. A recent model that CO2 signaling is mediated by PYL4/PYL5 ABA-receptors could not be supported here in two independent labs. We report a potent approach for real-time live-cell investigations of stress signaling.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Dióxido de Carbono / Proteínas Serina-Treonina Quinasas / Ácido Abscísico / Ciclopentanos / Oxilipinas / Acetatos Tipo de estudio: Prognostic_studies Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas de Plantas / Dióxido de Carbono / Proteínas Serina-Treonina Quinasas / Ácido Abscísico / Ciclopentanos / Oxilipinas / Acetatos Tipo de estudio: Prognostic_studies Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido