Plant cell surface immune receptor complex signaling

Wan, Wei‐Lin; Fröhlich, Katja; Pruitt, Rory; Nürnberger, Thorsten; Zhang, Lisha

doi:10.1016/j.pbi.2019.02.001

Cited by 95 publications

(143 citation statements)

References 98 publications

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“…In contrast, the AvrRpm1‐, AvrRpt2‐, and AvrRps5‐induced HR, which are activated by CNLs RPM1, RPS2, and RPS5, respectively, are still observed in nrg1a nrg1b mutants (Castel et al 2019). Similarly, the HR triggered by TNLs SOC3, CSA1, and RECOGNITION OF XOPQ 1 (Roq1), but not CNLs MLA7, MLA10, and RPM1, in tobacco requires NRG1 (Qi et al 2018; Castel et al 2019; Wan et al 2019a), indicating that NRG1 family members mainly function redundantly in TNL‐induced cell death, but not in CNL‐induced cell death. These findings are consistent with the studies on plant genomes that NRG1 co‐occurs with TNL genes (Bonardi et al 2011; Shao et al 2016; Gao et al 2018).…”

Section: Recent Discoveries Of the Activation Of Intracellular Nlrsmentioning

confidence: 99%

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Plant immune signaling: Advancing on two frontiers

Wang

Feng

Zhou

et al. 2020

JIPB

188

144

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Plants have evolved multiple defense strategies to cope with pathogens, among which plant immune signaling that relies on cell-surface localized and intracellular receptors takes fundamental roles. Exciting breakthroughs were made recently on the signaling mechanisms of pattern recognition receptors (PRRs) and intracellular nucleotide-binding site (NBS) and leucine-rich repeat (LRR) domain receptors (NLRs). This review summarizes the current view of PRRs activation, emphasizing the most recent discoveries about PRRs' dynamic regulation and signaling mechanisms directly leading to downstream molecular events including mitogen-activated protein kinase (MAPK) activation and calcium (Ca 2+ ) burst. Plants also have evolved intracellular NLRs to perceive the presence of specific pathogen effectors and trigger more robust immune responses. We also discuss the current understanding of the mechanisms of NLR activation, which has been greatly advanced by recent breakthroughs including structures of the first full-length plant NLR complex, findings of NLR sensor-helper pairs and novel biochemical activity of Toll/interleukin-1 receptor (TIR) domain.

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Section: Recent Discoveries Of the Activation Of Intracellular Nlrsmentioning

confidence: 99%

“…How plant TIR domains induce immune responses is an intriguing question. Recent studies discovered a biochemical activity of TIR that is essential for its immune signaling function (Horsefield et al 2019; Wan et al 2019a).…”

Section: Recent Discoveries Of the Activation Of Intracellular Nlrsmentioning

confidence: 99%

Plant immune signaling: Advancing on two frontiers

Wang

Feng

Zhou

et al. 2020

JIPB

188

144

View full text Add to dashboard Cite

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“…They serve to coordinate developmental processes, pathogen recognition, symbiotic interaction with beneficial microorganisms, or other aspects of environmental sensing (Osakabe et al, 2013). RLKs usually act in complexes consisting of a receptor and a coreceptor, and can form higher-order complexes that rearrange dynamically upon ligand perception (Wan et al, 2019). The same receptors can interact with different partners and be part of different complexes with different signaling specificity (Liebrand et al, 2014;Bücherl et al, 2017;Wan et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

“…RLKs usually act in complexes consisting of a receptor and a coreceptor, and can form higher-order complexes that rearrange dynamically upon ligand perception (Wan et al, 2019). The same receptors can interact with different partners and be part of different complexes with different signaling specificity (Liebrand et al, 2014;Bücherl et al, 2017;Wan et al, 2019). Most studies of RLK interaction initially relied on in vitro experiments, and could not provide insights into the spatial localization and complexity of interactions.…”

Section: Introductionmentioning

confidence: 99%

Over the rainbow: a practical guide for fluorescent protein selection in plant FRET experiments

Denay

Schultz

Hänsch

et al. 2019

Preprint

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One-sentence summaryWe compared the performances of several different fluorescent protein pairs to study membrane protein interaction in plants with FRET. Authors contributions:GD conceived the project and designed the experiments with input from all authors. GD prepared the figures and wrote the manuscript with the help of RS. GD and PS created expression vectors and performed measurements. GD, PS, and SH analyzed the data. SH and SWP provided critical help with lifetime measurement and analysis. All authors discussed the results and commented on the manuscript. AbstractReceptor-like kinases (RLK) and receptor-like proteins (RLP) often interact in a combinatorial manner depending on tissue identity, membrane domains, or endo-and exogenous cues, and the same RLKs or RLPs can generate different signaling outputs depending on the composition of the receptor complexes they are involved in. Investigation of their interaction partners in a spatial and dynamic way is therefore of prime interest to understand their functions. This is however limited by the technical complexity of assessing it in endogenous conditions. A solution to close this gap is to determine protein interaction directly in the relevant tissues at endogenous expression levels using Förster resonance energy transfer (FRET). The ideal fluorophore pair for FRET must, however, fulfil specific requirements: (i) the emission and excitation spectra of the donor and acceptor, respectively, must overlap; (ii) they should not interfere with proper folding, activity, or localization of the fusion proteins; (iii) they should be sufficiently photostable in plant cells. Furthermore, the donor must yield sufficient photon counts at near-endogenous protein expression levels. Although many fluorescent proteins were reported to be suitable for FRET experiments, only a handful were already described for applications in plants. Herein, we compare a range of fluorophores, assess their usability to study RLK interactions by FRET-based fluorescence lifetime imaging (FLIM) and explore their differences in FRET efficiency. Our analysis will help to select the optimal fluorophore pair for diverse FRET applications. be part of different complexes with different signaling specificity (Liebrand et al., 2014; Bücherl et al., 2017; Wan et al., 2019). Most studies of RLK interaction initially relied on in vitro experiments, and could not provide insights into the spatial localization and complexity of interactions. However, advances in imaging techniques now allow to study co-localization and interactions of RLKs in living plant cells (Somssich et al., 2015; Bücherl et al., 2017). In particular, Förster Resonance Energy Transfer (FRET) is an attractive technique as it allows to resolve protein-protein interactions in live plants in a cell-specific and dynamic manner (Somssich et al., 2015; Long et al., 2017; Weidtkamp-Peters and Stahl, 2017; Lampugnani et al., 2018). Determination of protein interaction by FRET relies on the energy transfer from a fluorescent donor to an accept...

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“…RLKs usually act in complexes consisting of a receptor and a co‐receptor, and can form higher‐order complexes that rearrange dynamically upon ligand perception (Wan, Fröhlich, Pruitt, Nürnberger, & Zhang, ). The same receptors can interact with different partners and be a part of different complexes with different signaling specificity (Bücherl et al, ; Liebrand, Burg, & Joosten, ; Wan et al, ). Most studies of RLK interaction initially relied on in vitro experiments and could not provide insights into the spatial localization and complexity of interactions.…”

Section: Introductionmentioning

confidence: 99%

Over the rainbow: A practical guide for fluorescent protein selection in plant FRET experiments

et al. 2019

View full text Add to dashboard Cite

Receptor‐like kinases (RLK) and receptor‐like proteins (RLP) often interact in a combinatorial manner depending on tissue identity, membrane domains, or endo‐ and exogenous cues, and the same RLKs or RLPs can generate different signaling outputs depending on the composition of the receptor complexes they are involved in. Investigation of their interaction partners in a spatial and dynamic way is therefore of prime interest to understand their functions. This is, however, limited by the technical complexity of assessing it in endogenous conditions. A solution to close this gap is to determine protein interaction directly in the relevant tissues at endogenous expression levels using Förster resonance energy transfer (FRET). The ideal fluorophore pair for FRET must, however, fulfil specific requirements: (a) The emission and excitation spectra of the donor and acceptor, respectively, must overlap; (b) they should not interfere with proper folding, activity, or localization of the fusion proteins; (c) they should be sufficiently photostable in plant cells. Furthermore, the donor must yield sufficient photon counts at near‐endogenous protein expression levels. Although many fluorescent proteins were reported to be suitable for FRET experiments, only a handful were already described for applications in plants. Herein, we compare a range of fluorophores, assess their usability to study RLK interactions by FRET‐based fluorescence lifetime imaging (FLIM) and explore their differences in FRET efficiency. Our analysis will help to select the optimal fluorophore pair for diverse FRET applications.

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Plant cell surface immune receptor complex signaling

Cited by 95 publications

References 98 publications

Plant immune signaling: Advancing on two frontiers

Plant immune signaling: Advancing on two frontiers

Over the rainbow: a practical guide for fluorescent protein selection in plant FRET experiments

Over the rainbow: A practical guide for fluorescent protein selection in plant FRET experiments

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