Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity

Kadota, Yasuhiro, Sklenar, Jan, Derbyshire, Paul, Stransfeld, Lena, Asai, Shuta, Ntoukakis, Vardis, Jones, Jonathan Dg, Shirasu, Ken, Menke, Frank ORCID: https://orcid.org/0000-0003-2490-4824, Jones, Alexandra and Zipfel, Cyril (2014) Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity. Molecular Cell, 54 (1). pp. 43-55. ISSN 1097-2765

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Abstract

The rapid production of reactive oxygen species (ROS) burst is a conserved signaling output in immunity across kingdoms. In plants, perception of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors (PRRs) activates the NADPH oxidase RBOHD by hitherto unknown mechanisms. Here, we show that RBOHD exists in complex with the receptor kinases EFR and FLS2, which are the PRRs for bacterial EF-Tu and flagellin, respectively. The plasma-membrane-associated kinase BIK1, which is a direct substrate of the PRR complex, directly interacts with and phosphorylates RBOHD upon PAMP perception. BIK1 phosphorylates different residues than calcium-dependent protein kinases, and both PAMP-induced BIK1 activation and BIK1-mediated phosphorylation of RBOHD are calcium independent. Importantly, phosphorylation of these residues is critical for the PAMP-induced ROS burst and antibacterial immunity. Our study reveals a rapid regulatory mechanism of a plant RBOH, which occurs in parallel with and is essential for its paradigmatic calcium-based regulation.

Item Type:	Article
Additional Information:	Copyright © 2014 Elsevier Inc. All rights reserved.
Uncontrolled Keywords:	amino acid sequence,arabidopsis,arabidopsis proteins,cell line,enzyme activation,flagellin,gene expression regulation, enzymologic,gene expression regulation, plant,immunity, innate,ligands,molecular sequence data,multienzyme complexes,nadph oxidase,peptide elongation factor tu,phosphorylation,plant immunity,plant stomata,protein kinases,protein-serine-threonine kinases,reactive oxygen species,receptors, immunologic,receptors, pattern recognition,signal transduction,tobacco
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > The Sainsbury Laboratory
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	04 Jul 2014 12:42
Last Modified:	24 Oct 2022 06:24
URI:	https://ueaeprints.uea.ac.uk/id/eprint/48855
DOI:	10.1016/j.molcel.2014.02.021

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