SCHENGEN receptor module drives localized ROS production and lignification in plant roots. Fujita, S., De Bellis, D., Edel, K. H, Köster, P., Andersen, T. G., Schmid-Siegert, E., Dénervaud Tendon, V., Pfister, A., Marhavý, P., Ursache, R., Doblas, V. G, Barberon, M., Daraspe, J., Creff, A., Ingram, G., Kudla, J., & Geldner, N. The EMBO Journal, 39(9):e103894, May, 2020. Publisher: John Wiley & Sons, Ltd![SCHENGEN receptor module drives localized ROS production and lignification in plant roots [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 2 downloads Abstract Production of reactive oxygen species (ROS) by NADPH oxidases (NOXs) impacts many processes in animals and plants, and many plant receptor pathways involve rapid, NOX-dependent increases of ROS. Yet, their general reactivity has made it challenging to pinpoint the precise role and immediate molecular action of ROS. A well-understood ROS action in plants is to provide the co-substrate for lignin peroxidases in the cell wall. Lignin can be deposited with exquisite spatial control, but the underlying mechanisms have remained elusive. Here, we establish a kinase signaling relay that exerts direct, spatial control over ROS production and lignification within the cell wall. We show that polar localization of a single kinase component is crucial for pathway function. Our data indicate that an intersection of more broadly localized components allows for micrometer-scale precision of lignification and that this system is triggered through initiation of ROS production as a critical peroxidase co-substrate.
@article{fujita_schengen_2020,
title = {{SCHENGEN} receptor module drives localized {ROS} production and lignification in plant roots},
volume = {39},
issn = {0261-4189},
url = {https://www.embopress.org/doi/full/10.15252/embj.2019103894},
doi = {10/gjct3x},
abstract = {Abstract Production of reactive oxygen species (ROS) by NADPH oxidases (NOXs) impacts many processes in animals and plants, and many plant receptor pathways involve rapid, NOX-dependent increases of ROS. Yet, their general reactivity has made it challenging to pinpoint the precise role and immediate molecular action of ROS. A well-understood ROS action in plants is to provide the co-substrate for lignin peroxidases in the cell wall. Lignin can be deposited with exquisite spatial control, but the underlying mechanisms have remained elusive. Here, we establish a kinase signaling relay that exerts direct, spatial control over ROS production and lignification within the cell wall. We show that polar localization of a single kinase component is crucial for pathway function. Our data indicate that an intersection of more broadly localized components allows for micrometer-scale precision of lignification and that this system is triggered through initiation of ROS production as a critical peroxidase co-substrate.},
number = {9},
urldate = {2021-06-21},
journal = {The EMBO Journal},
author = {Fujita, Satoshi and De Bellis, Damien and Edel, Kai H and Köster, Philipp and Andersen, Tonni Grube and Schmid-Siegert, Emanuel and Dénervaud Tendon, Valérie and Pfister, Alexandre and Marhavý, Peter and Ursache, Robertas and Doblas, Verónica G and Barberon, Marie and Daraspe, Jean and Creff, Audrey and Ingram, Gwyneth and Kudla, Jörg and Geldner, Niko},
month = may,
year = {2020},
note = {Publisher: John Wiley \& Sons, Ltd},
keywords = {Casparian strips, extracellular diffusion barriers, lignin, localized ROS production, polarized signaling},
pages = {e103894},
}
Downloads: 2
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Yet, their general reactivity has made it challenging to pinpoint the precise role and immediate molecular action of ROS. A well-understood ROS action in plants is to provide the co-substrate for lignin peroxidases in the cell wall. Lignin can be deposited with exquisite spatial control, but the underlying mechanisms have remained elusive. Here, we establish a kinase signaling relay that exerts direct, spatial control over ROS production and lignification within the cell wall. We show that polar localization of a single kinase component is crucial for pathway function. 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