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Fine-tuning of RBOHF activity is achieved by differential phosphorylation and Ca2+ binding

• RBOHF from Arabidopsis thaliana represents a multifunctional NADPH oxidase regulating biotic and abiotic stress tolerance, developmental processes and guard cell aperture. The molecular components and mechanisms determining RBOHF activity remain to be elucidated. • Here we combined protein interac...

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Bibliographic Details
Published in:The New phytologist 2019-03, Vol.221 (4), p.1935-1949
Main Authors: Han, Jian-Pu, Köster, Philipp, Drerup, Maria M., Scholz, Martin, Li, Shizhen, Edel, Kai H., Hashimoto, Kenji, Kuchitsu, Kazuyuki, Hippler, Michael, Kudla, Jörg
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Language:English
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Summary:• RBOHF from Arabidopsis thaliana represents a multifunctional NADPH oxidase regulating biotic and abiotic stress tolerance, developmental processes and guard cell aperture. The molecular components and mechanisms determining RBOHF activity remain to be elucidated. • Here we combined protein interaction studies, biochemical and genetic approaches, and pathway reconstitution analyses to identify and characterize proteins that confer RBOHF regulation and elucidated mechanisms that adjust RBOHF activity. • While the Ca2+ sensor-activated kinases CIPK11 and CIPK26 constitute alternative paths for RBOHF activation, the combined activity of CIPKs and the kinase open stomata 1 (OST1) triggers complementary activation of this NADPH oxidase, which is efficiently counteracted through dephosphorylation by the phosphatase ABI1. Within RBOHF, several distinct phosphorylation sites (p-sites) in the N-terminus of RBOHF appear to contribute individually to activity regulation. • These findings identify RBOHF as a convergence point targeted by a complex regulatory network of kinases and phosphatases. We propose that this allows for fine-tuning of plant reactive oxygen species (ROS) production by RBOHF in response to different stimuli and in diverse physiological processes.
ISSN:0028-646X
1469-8137
DOI:10.1111/nph.15543