The Arabidopsis Protein Phosphatase PP2C38 Negatively Regulates the Central Immune Kinase BIK1

PLoS Pathogens

Joachim Uhrig¹  Jian-Min Zhou²  Xiangxiu Liang²  Silke Robatzek³  Denise Altenbach³  Christoph A. Bücherl⁴  Alberto P. Macho⁴  Roda Niebergall⁴  Dan Maclean⁴  Daniel Couto⁴  Frank Menke⁴  Vardis Ntoukakis⁴  Paul Derbyshire⁴  Cyril Zipfel⁴  Jan Sklenar⁴ 

[1] Botanical Institute III, University of Cologne, Cologne, Germany;Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China;Max-Planck-Institute for Plant Breeding Research, Cologne, Germany;The Sainsbury Laboratory, Norwich Research Park, Norwich, United Kingdom

关键词: Phosphorylation;    Arabidopsis thaliana;    Phosphatases;    Immune receptor signaling;    Co-immunoprecipitation;    Leaves;    Membrane proteins;    Two-hybrid screening;   

DOI  :  10.1371/journal.ppat.1005811

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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.

【 授权许可】

CC BY