The Arabidopsis protein phosphatase PP2C38 negatively regulates the central immune kinase BIK1

Couto, Daniel, Niebergall, Roda, Liang, Xiangxiu, Buecherl, Christoph, Sklenar, Jan, Macho, Alberto, Ntoukakis, Vardis, Derbyshire, Paul, Altenbach, Denise, MacLean, Dan, Robatzek, Silke, Uhrig, Joachim, Menke, Frank ORCID: https://orcid.org/0000-0003-2490-4824, Zhou, Jian-Min and Zipfel, Cyril (2016) The Arabidopsis protein phosphatase PP2C38 negatively regulates the central immune kinase BIK1. PLoS Pathogens, 12 (8). ISSN 1553-7366

Preview	PDF (Accepted manuscript) - Accepted Version Available under License Creative Commons Attribution. Download (364kB) | Preview
Preview	PDF (Published_Version) - Published Version Available under License Creative Commons Attribution. Download (5MB) | Preview

Abstract

Plants recognize pathogen-associated molecular patterns (PAMPs) via cell surface-localized pattern recognition receptors (PRRs), leading to PRR-triggered immunity (PTI). The Arabidopsis cytoplasmic kinase BIK1 is a downstream substrate of several PRR complexes. How plant PTI is negatively regulated is not fully understood. Here, we identify the protein phosphatase PP2C38 as a negative regulator of BIK1 activity and BIK1-mediated immunity. PP2C38 dynamically associates with BIK1, as well as with the PRRs FLS2 and EFR, but not with the co-receptor BAK1. PP2C38 regulates PAMP-induced BIK1 phosphorylation and impairs the phosphorylation of the NADPH oxidase RBOHD by BIK1, leading to reduced oxidative burst and stomatal immunity. Upon PAMP perception, PP2C38 is phosphorylated on serine 77 and dissociates from the FLS2/EFR-BIK1 complexes, enabling full BIK1 activation. Together with our recent work on the control of BIK1 turnover, this study reveals another important regulatory mechanism of this central immune component.

Item Type:	Article
Additional Information:	© 2016 Couto et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Faculty \ School:	Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	24 Sep 2016 00:06
Last Modified:	22 Oct 2022 01:21
URI:	https://ueaeprints.uea.ac.uk/id/eprint/59820
DOI:	10.1371/journal.ppat.1005811

Downloads

Actions (login required)

View Item