A chemical and synthetic biology approach to control plant membrane receptor kinase signaling
Ontology highlight
ABSTRACT:
ORGANISM(S): Arabidopsis thaliana
PROVIDER: GSE136177 | GEO | 2021/06/10
REPOSITORIES: GEO
Similar Datasets
Project description:Receptor kinases (RKs) play fundamental roles in extracellular sensing to regulate development and stress responses across kingdoms. In plants, leucine-rich repeat receptor kinases (LRR-RKs) function primarily as peptide receptors that regulate myriad aspects of plant development and response to external stimuli. Extensive phosphorylation of LRR-RK cytoplasmic domains is among the earliest detectable responses following ligand perception, and reciprocal transphosphorylation between a receptor and its co-receptor is proposed to activate the receptor complex. Originally conceived based on characterization of the brassinosteroid receptor, the prevalence of complex activation via reciprocal transphosphorylation across the plant RK family has not been tested. Using the LRR-RK ELONGATION FACTOR TU RECEPTOR (EFR) as a model RK, we set out to understand the steps critical for activating RK complexes. The EFR cytoplasmic domain is an active protein kinase in vitro and is phosphorylated in a ligand-dependent manner in vivo. Nevertheless, catalytically deficient EFR variants are functional in anti-bacterial immunity. These results reveal a non-catalytic role for the EFR cytoplasmic domain in triggering immune signaling and indicate that reciprocal transphoshorylation is not a ubiquitous requirement for LRR-RK complex activation. Rather, our analysis of EFR along with a detailed survey of the literature suggests a distinction between LRR-RK complexes with RD- versus non-RD-type protein kinase domains. Based on newly identified phosphorylation sites that regulate the activation state of the EFR complex in vivo, we propose that LRR-RK complexes containing a non-RD-type protein kinase may be activated by an allosteric mechanism triggered by activation segment phosphorylation and possibly involving conformational changes of the protein kinase domain of the ligand-binding receptor.
2021-10-27 | PXD025597 | Pride
Project description:Plant cell surface receptors sense microbial pathogens by recognizing microbial structures called pathogen or microbe-associated molecular patterns (PAMPs/MAMPs). There are two major types of plant pattern recognition receptors: 1. Leucine-rich repeat receptor proteins (LRR-RP) and LRR receptor kinases (LRR-RK) and 2. Plant receptor proteins and receptor kinases carrying ectopic lysin motifs (LysM-RP and LysM-RK). In this study, Arabidopsis thaliana responses to three different MAMPs, flg22, nlp20, chitin (C6), via their corresponding receptor types, FLS2 (LRR-RK), RLP23 (LRR-RP), CERK1 (LysM-RK) were compared. Our RNA-seq results indicate that a core set of defense-related genes can be activated through perception of different MAMPs. However, there are also notable differences in the transcriptional changes in response to the various elicitors; flg22 causes broader transcriptome changes than nlp20 and C6, and C6 does not cause late transcriptome changes.
2019-06-21 | GSE133053 | GEO
Project description:Plant receptor kinases (RKs) are critical for transmembrane signaling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is a unique RK that recognizes a family of immunomodulatory peptides called SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) and activates pattern-triggered immunity (PTI) responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. In this study, we present the cryo-EM structure of a ternary complex consisting of the extracellular leucine-rich repeat of MIK2 (MIK2LRR), SCOOP12, and the extracellular LRR of the co-receptor BAK1 (BAK1LRR) at a resolution of 3.34 Å. The structure reveals that a DNHH motif in MIK2LRR plays a critical role in specifically recognizing the highly conserved SxS motif of SCOOP12. Furthermore, the structure demonstrates that N-glycans at MIK2LRRAsn410 directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRRN410D, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and significantly impairs the assembly of the MIK2LRR-SCOOP12-BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2N410D substantially compromises SCOOP12-triggered immune responses in plants. Collectively, these findings elucidate the mechanism underlying the loose specificity of SCOOP recognition by MIK2 and reveal an unprecedented mechanism by which N-glycosylation modification of LRR-RK promotes receptor activation.
2024-10-22 | PXD054177 | Pride
Project description:Plant receptor kinases (RKs) are critical for transmembrane signaling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is a unique RK that recognizes a family of immunomodulatory peptides called SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) and activates pattern-triggered immunity (PTI) responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. In this study, we present the cryo-EM structure of a ternary complex consisting of the extracellular leucine-rich repeat of MIK2 (MIK2LRR), SCOOP12, and the extracellular LRR of the co-receptor BAK1 (BAK1LRR) at a resolution of 3.34 Å. The structure reveals that a DNHH motif in MIK2LRR plays a critical role in specifically recognizing the highly conserved SxS motif of SCOOP12. Furthermore, the structure demonstrates that N-glycans at MIK2LRRAsn410 directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRRN410D, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and significantly impairs the assembly of the MIK2LRR-SCOOP12-BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2N410D substantially compromises SCOOP12-triggered immune responses in plants. Collectively, these findings elucidate the mechanism underlying the loose specificity of SCOOP recognition by MIK2 and reveal an unprecedented mechanism by which N-glycosylation modification of LRR-RK promotes receptor activation.
2024-10-22 | PXD054149 | Pride
Project description:Plants deploy cell surface and intracellular leucine rich-repeat domain (LRR) immune receptors to detect pathogens. LRR receptor kinases (LRR-RKs) and LRR receptor proteins (LRR-RPs) recognise microbe-derived molecules to elicit pattern-triggered immunity (PTI), whereas nucleotide-binding LRR (NLR) proteins detect microbial effectors inside cells to confer effector-triggered immunity (ETI). Although PTI and ETI are initiated in different host cell compartments, they rely on the transcriptional activation of similar sets of genes, suggesting pathway convergence upstream of nuclear events. We report that PTI triggered by Arabidopsis LRR-RP (RLP23) requires signalling-competent dimers of the lipase-like proteins EDS1 and PAD4, and ADR1-family helper NLRs, which are all components of ETI. The cell surface LRR-RK SOBIR1 links RLP23 with EDS1, PAD4 and ADR1 proteins, suggesting formation of constitutive supramolecular complexes containing PTI receptors and transducers at the inner side of the plasma membrane.
2021-07-05 | PXD026120 | Pride
Project description:To effectively manage resources, regulatory cross-talk between biological processes within an organism is essential. An emerging area in plant research focuses on antagonism between regulatory systems controlling growth/development and those governing immunity. Such crosstalk represents a point of vulnerability for pathogens to exploit. Here we show that the notorious potato blight pathogen Phytophthora infestans promotes a growth and development pathway in order to antagonise plant immunity. AVR2, an effector protein secreted by P. infestans, has been shown to interact with potato BSL1, a putative phosphatase implicated in brassinosteroid hormone signalling. Plants expressing AVR2 exhibit transcriptional and phenotypic overlaps with an over-active brassinosteroid signalling pathway, and have compromised immunity. The activity of AVR2 leads to up-regulation of a functional orthologue of AtHBI1, known to facilitate cross-talk between the brassinosteroid pathway and immune signalling in Arabidopsis. Transient expression of potato HBI1-like compromises immunity and enhances leaf colonisation by P. infestans. Knowledge of how pathogens manipulate regulatory cross-talk governing resource allocation in plants will inform crop breeding efforts of the future; helping to maximise both yield and resistance to ensure food security as pressure on our agricultural systems increases.
2017-03-01 | E-MTAB-3854 | biostudies-arrayexpress
Project description:Plant height is a critical constituent of plant architecture. Rice (Oryza sativa) plants have the potential to undergo rapid internodal elongation, which determines plant height. A number of physiological studies have proved that gibberellin is involved in internode elongation. Leucine-rich repeat receptor-like kinases (LRR-RLKs) are the largest subfamily of transmembrane receptor-like kinases in plants. Plant LRR-RLKs play important functions in mediating a variety of cellular processes and regulating responses to environmental signals. LRK1, a PSK receptor homolog, is a member of the LRR-RLK family. In the present study, differences in ectopic expression of LRK1 were consistent with extent of rice internode elongation. Analyses of gene expression demonstrated that LRK1 restricts gibberellin responsiveness during the internode elongation process by down-regulation of the gibberellin biosynthetic gene, ent-KAURENE OXIDASE (OsKO2).
2012-02-12 | GSE35729 | GEO
Project description:Leucine-rich repeat (LRR) domains are evolutionarily conserved in proteins that function in development and immunity. Somatic recombination of LRR sequences evolved to create diversity in jawless vertebrate adaptive immunity, yet the role repetitive LRR-encoding exons in humans remains unknown. We performed this RNA Seq study to understand how alternative splicing of NOD-like receptors (NLRs) at the locus encoding a LRR domain can regulate NLRs function, with a focus on NLRP3.
2019-06-09 | GSE117206 | GEO
Project description:Plant height is a critical constituent of plant architecture. Rice (Oryza sativa) plants have the potential to undergo rapid internodal elongation, which determines plant height. A number of physiological studies have proved that gibberellin is involved in internode elongation. Leucine-rich repeat receptor-like kinases (LRR-RLKs) are the largest subfamily of transmembrane receptor-like kinases in plants. Plant LRR-RLKs play important functions in mediating a variety of cellular processes and regulating responses to environmental signals. LRK1, a PSK receptor homolog, is a member of the LRR-RLK family. In the present study, differences in ectopic expression of LRK1 were consistent with extent of rice internode elongation. Analyses of gene expression demonstrated that LRK1 restricts gibberellin responsiveness during the internode elongation process by down-regulation of the gibberellin biosynthetic gene, ent-KAURENE OXIDASE (OsKO2). Leaf tissues of 6-week-old LRK1 060615 transgenic rice and control 9311 rice (10 plants each) were selected.
2012-02-12 | E-GEOD-35729 | biostudies-arrayexpress
Project description:An important branch of plant immunity involves the recognition of pathogens by the NB-LRR proteins encoded by disease resistance genes. However, signaling events downstream of NB-LRR activation are poorly understood. We have analyzed the Arabidopsis translatome using ribosome affinity purification and RNAseq. Our results show that the translational status of hundreds of genes are differentially affected upon activation of the NB-LRR protein RPM1, showing an overall pattern of a switch away from growth-related activities to defense. Among these is the central translational regulator and growth promoter, TOR kinase. Suppression of TOR expression leads to increased resistance to pathogens while overexpression of TOR results in increased susceptibility, indicating an important role for translational control in the growth to defense switch. Furthermore, we show that several additional genes whose mRNAs are translationally regulated, including BIG, CCT2 and CIPK5, are required for plant innate immunity, identifying novel actors in plant defense.
2017-03-06 | GSE75640 | GEO