Identification of novel regulators of the NADPH oxidase RBOHD during plant immunity
Y. KADOTA (1), Y. Goto (2), H. Matsui (3), J. Sklenar (4), P. Derbyshire (4), F. Menke (4), H. Nakagami (3), C. Zipfel (4), K. Shirasu (2) (1) RIKEN CSRS, Plant Immunity Research Group,, Japan; (2) RIKEN CSRS, Plant Immunity Research Group,, Japan; (3) RIKEN CSRS, Plant Proteomics Research Unit, Japan; (4) The Sainsbury Laboratory, United Kingdom; (5) RIKEN CSRS, Plant Proteomics Research Unit, Japan

The production of reactive oxygen species (ROS) is a conserved signaling output in immunity across kingdoms. In the model plant Arabidopsis thaliana, perception of pathogen-associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors (PRRs) activates the NADPH oxidase RBOHD. ROS has direct antimicrobial properties, but also serves as signaling molecules to modulate downstream immune responses. However, its production has to be tightly controlled to avoid detrimental effects on host cells. Thus, it must be produced in the right amount, at the right place and at the right time. To understand the regulatory mechanism of RBOHD, we employed co-immunoprecipitation coupled with mass spectrometry analyses to identify novel interactors of RBOHD. The candidate interactors include (1) proteins that are known to form complex with PRRs, (2) proteins previously known to be part of PAMP-induced detergent resistant membrane compartments, and (3) proteins that share the same domains as regulators of animal NADPH oxidases. The role of these proteins in PAMP-induced ROS production has been examined by transient over-expression in the heterologous plant Nicotiana benthamiana. The possible roles of these candidates with respect to RBOHD regulation will be discussed.

Abstract Number: P17-541
Session Type: Poster