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Fine-tuning of RBOHF activity is achieved by differential phosphorylation and Ca2+ binding
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Fine-tuning of RBOHF activity is achieved by differential phosphorylation and Ca2+ binding
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Journal Article
Fine-tuning of RBOHF activity is achieved by differential phosphorylation and Ca2+ binding
2019
Overview
• 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.
Publisher
Wiley,Wiley Subscription Services, Inc
Subject
/ Ca2
/ Calcium
/ CBL/CIPK
/ Kinases
/ NAD(P)H oxidase (H2O2-forming)
/ OST1
/ Oxidase
/ phosphotransferases (kinases)
/ Proteins
/ RBOH
/ reactive oxygen species (ROS)
/ Stomata
/ Tuning
