Regulation of the NADPH Oxidase RBOHD During Plant Immunity

被引:467
作者
Kadota, Yasuhiro [1 ]
Shirasu, Ken [1 ]
Zipfel, Cyril [2 ]
机构
[1] RIKEN, Ctr Sustainable Resource Sci, Plant Immun Res Grp, Tsurumi ku, Yokohama, Kanagawa 2300045, Japan
[2] Sainsbury Lab, Norwich NR4 7UH, Norfolk, England
基金
欧洲研究理事会; 日本学术振兴会;
关键词
Calcium; Innate immunity; Pathogen-associated molecular patterns; Pattern recognition receptors; Phosphorylation; Reactive oxygen species; OXYGEN SPECIES PRODUCTION; POSITIVE FEEDBACK-REGULATION; APOPLASTIC OXIDATIVE BURST; ROS-PRODUCING ACTIVITY; PROTEIN-KINASE CIPK26; CELL-DEATH; CYTOPLASMIC KINASE; INNATE IMMUNITY; SIGNALING PATHWAYS; DEFENSE RESPONSES;
D O I
10.1093/pcp/pcv063
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Pathogen recognition induces the production of reactive oxygen species (ROS) by NADPH oxidases in both plants and animals. ROS have direct antimicrobial properties, but also serve as signaling molecules to activate further immune outputs. However, ROS production has to be tightly controlled to avoid detrimental effects on host cells, but yet must be produced in the right amount, at the right place and at the right time upon pathogen perception. Plant NADPH oxidases belong to the respiratory burst oxidase homolog (RBOH) family, which contains 10 members in the model plant Arabidopsis thaliana. The perception of pathogen-associated molecular patterns (PAMPs) by pattern recognition receptors (PRRs) leads to a rapid, specific and strong production of ROS, which is dependent on RBOHD. RBOHD is mainly controlled by Ca2+ via direct binding to EF-hand motifs and phosphorylation by Ca2+-dependent protein kinases. Recent studies have, however, revealed a critical role for a Ca2+-independent regulation of RBOHD. The plasma membrane-associated cytoplasmic kinase BIK1 (BOTRYTIS-INDUCED KINASE1), which is a direct substrate of the PRR complex, directly interacts with and phosphorylates RBOHD upon PAMP perception. Impairment of these phosphorylation events completely abolishes the function of RBOHD in immunity. These results suggest that RBOHD activity is tightly controlled by multilayered regulations. In this review, we summarize recent advances in our understanding of the regulatory mechanisms controlling RBOHD activation.
引用
收藏
页码:1472 / 1480
页数:9
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