Guozhi Bi

China Agricultural University

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Jian‐Min Zhou

State Key Laboratory of Plant Genomics

M.H.A.J. Joosten

Wageningen University & Research

Xiaojuan Zhang

Shaanxi University of Technology

Jelle Postma

Radboud University Nijmegen

Zhaoyang Zhou

China Agricultural University

Silke Robatzek

Sainsbury Laboratory

Thomas W. H. Liebrand

University of California, Davis

Ruby R. Bye

Wageningen University & Research

Aranka M. van der Burgh

Wageningen University & Research

Meijuan Hu

State Key Laboratory of Plant Genomics

Cooperative Institutions

Chinese Academy of Sciences

University of Chinese Academy of Sciences

Institute of Genetics and Developmental Biology

State Key Laboratory of Plant Genomics

China Agricultural University

Wageningen University & Research

Ministry of Agriculture and Rural Affairs

Center for Excellence in Molecular Plant Sciences

Tsinghua University

Sainsbury Laboratory

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Luciferase Complementation Assay for Protein‐Protein Interactions in Plants

Current Protocols in Plant Biology (2018)

Zhaoyang Zhou Guozhi Bi Jianmin Zhou

Constitutive and dynamic protein-protein interactions are fundamental to all aspects of cellular processes. Compared to other techniques measuring protein-protein interactions in plants, the luciferase complementation assay has a number of advantages: it detects plant protein-protein interactions in real time, requires little hands-on manipulation of samples, is highly quantitative, has extremely low background, and can be easily scaled up for high-throughput interactome studies. Here, we describe a protocol that includes two alternate data collection methods to quantify luminescence results based on Agrobacterium-mediated transient luciferase expression in Nicotiana benthamiana. One data collection method employs a charge-coupled device imaging system that allows the interactions to be presented as images, and the other employs a luminometer, which enables the assay to be conducted in a 96-well plate. Technical parameters related to frequently encountered problems and common errors, presented here, are important for performing this assay successfully. © 2018 by John Wiley & Sons, Inc.

Interactome

Protein-fragment complementation assay

10.1002/cppb.20066

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Citations (128)

MAP Kinase Signaling Pathways: A Hub of Plant-Microbe Interactions

Cell Host & Microbe (2017)

Guozhi Bi Jian‐Min Zhou

Identification

10.1016/j.chom.2017.02.004

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Citations (80)

The Cf-4 receptor-like protein associates with the BAK1 receptor-like kinase to initiate receptor endocytosis and plant immunity

bioRxiv (Cold Spring Harbor Laboratory) (2015)

Jelle Postma Thomas W. H. Liebrand Guozhi Bi Alexandre Evrard Ruby R. Bye

Summary The first layer of plant immunity is activated by cell surface receptor-like kinases (RLKs) and proteins (RLPs) that detect infectious pathogens. Constitutive interaction with the RLK SUPPRESSOR OF BIR1 (SOBIR1) contributes to RLP stability and kinase activity. As RLK activation requires transphosphorylation with a second associated RLK, it remains elusive how RLPs initiate downstream signaling. To address this, we investigated functioning of Cf RLPs that mediate immunity of tomato against Cladosporium fulvum . We employed live-cell imaging and co-immunoprecipitation in tomato and Nicotiana benthamiana to investigate the requirement of associated kinases for Cf activity and ligand-induced subcellular trafficking of Cf-4. Upon elicitation with the matching effector ligands Avr4 and Avr9, BRI1-ASSOCIATED KINASE 1 (BAK1) associates with Cf-4 and Cf-9. Furthermore, Cf-4 that interacts with SOBIR1 at the plasma membrane, is recruited to late endosomes after elicitation. Significantly, BAK1 is required for Avr4-triggered endocytosis, effector-triggered defenses in Cf-4 plants and resistance of tomato against C. fulvum . Our observations indicate that RLP-mediated immune signaling and endocytosis require ligand-induced recruitment of BAK1, reminiscent of BAK1 interaction and subcellular fate of the FLAGELLIN SENSING 2 RLK. This reveals that diverse classes of cell surface immune receptors share common requirements for signaling initiation and endocytosis.

10.1101/019471

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Citations (8)

Bacterial Effectors Induce Oligomerization of Immune Receptor ZAR1 In Vivo

Molecular Plant (2020)

Meijuan Hu Jinfeng Qi Guozhi Bi Jian‐Min Zhou

10.1016/j.molp.2020.03.004

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Citations (68)

SOBIR1-mediated immunity requires conserved tyrosine residues in its kinase domain

Aranka M. van der Burgh Guozhi Bi Jelle Postma Silke Robatzek M.H.A.J. Joosten

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The ZAR1 resistosome is a calcium-permeable channel triggering plant immune signaling

Cell (2021)

Guozhi Bi Min Su Nan Li Yu Liang Song Dang

10.1016/j.cell.2021.05.003

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Citations (422)

The OXI1 kinase regulates plant immunity by linking microbial pattern-induced ROS burst to MAPK activation

The Plant Cell (2024)

Miaomiao Ma Pan Wang Rubin Chen Mei Bai Zhuoyuan He

Abstract Plant cell-surface-localized pattern recognition receptors (PRRs) recognize microbial patterns and activate pattern-triggered immunity (PTI). Typical PTI responses include reactive oxygen species (ROS) burst controlled by the NADPH oxidase RESPIRATORY BURST OXIDASE HOMOLOGUE D (RbohD) and activation of the mitogen-activated protein kinase (MAPK) cascade composed of MAPKKK3/5-MKK4/5-MPK3/6. However, the mechanisms through which PRRs regulate and coordinate these immune responses are not fully understood. Here, we showed that Arabidopsis thaliana OXIDATIVE SIGNAL-INDUCIBLE1 (OXI1), a kinase known to be activated by ROS, is involved in the LYK5-CERK1 receptor complex, which recognizes fungal cell wall-derived chitin. The oxi1 mutant exhibits enhanced susceptibility to various pathogens and reduced chitin-induced MAPK activation and ROS burst. We showed that chitin induces the phosphorylation of OXI1 in an RbohD-dependent manner. H2O2 and chitin treatment causes the oxidation of OXI1 at Cys104 and Cys205, which is essential for the kinase activity of OXI1. These oxidation sites are required for chitin-induced MAPK activation and disease resistance. Activated OXI1 directly phosphorylates MAPKKK5 to regulate MAPK activation. Additionally, OXI1 phosphorylates RbohD, suggesting that it may activate RbohD to promote ROS burst to further enhance the long-term MAPK activation. Together, our findings reveal a pathway linking PRR-mediated ROS production to MAPK activation through OXI1.

Respiratory burst

10.1093/plcell/koae311

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Citations (1)

Receptor-Like Cytoplasmic Kinases Directly Link Diverse Pattern Recognition Receptors to the Activation of Mitogen-Activated Protein Kinase Cascades in Arabidopsis

The Plant Cell (2018)

Guozhi Bi Zhaoyang Zhou Weibing Wang Lin Li Shaofei Rao

Plants deploy numerous cell surface-localized pattern-recognition receptors (PRRs) to perceive host- and microbe-derived molecular patterns that are specifically released during infection and activate defense responses. The activation of the mitogen-activated protein kinases MPK3, MPK4, and MPK6 (MPK3/4/6) is a hallmark of immune system activation by all known PRRs and is crucial for establishing disease resistance. The MAP kinase kinase kinase (MAPKKK) MEKK1 controls MPK4 activation, but the MAPKKKs responsible for MPK3/6 activation downstream of diverse PRRs and how the perception of diverse molecular patterns leads to the activation of MAPKKKs remain elusive. Here, we show that two highly related MAPKKKs, MAPKKK3 and MAPKKK5, mediate MPK3/6 activation by at least four PRRs and confer resistance to bacterial and fungal pathogens in Arabidopsis thaliana The receptor-like cytoplasmic kinases VII (RLCK VII), which act downstream of PRRs, directly phosphorylate MAPKKK5 Ser-599, which is required for pattern-triggered MPK3/6 activation, defense gene expression, and disease resistance. Surprisingly, MPK6 further phosphorylates MAPKKK5 Ser-682 and Ser-692 to enhance MPK3/6 activation and disease resistance, pointing to a positive feedback mechanism. Finally, MEKK1 Ser-603 is phosphorylated by both RLCK VII and MPK4, which is required for pattern-triggered MPK4 activation. These findings illustrate central mechanisms by which multiple PRRs activate MAPK cascades and disease resistance.

10.1105/tpc.17.00981

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Citations (260)

The cytosolic thiol peroxidase PRXIIB is an intracellular sensor for H2O2 that regulates plant immunity through a redox relay

Figshare (2022)

Guozhi Bi Man Hu Ling Fu Xiaojuan Zhang Jiayang Li

Main figures, Extended Data figures, and supplementary information

Plant Immunity

10.6084/m9.figshare.20524941

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The cytosolic thiol peroxidase PRXIIB is an intracellular sensor for H2O2 that regulates plant immunity through a redox relay