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Sessile plants encode a large number of small peptides and cell surface-resident receptor kinases, most of which have unknown functions. Here, we report that the Arabidopsis receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) recognizes the conserved signature motif of SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) from Brassicaceae plants as well as proteins present in fungal Fusarium spp. and bacterial Comamonadaceae , and elicits various immune responses. SCOOP signature peptides trigger immune responses and altered root development in a MIK2-dependent manner with a sub-nanomolar sensitivity. SCOOP12 directly binds to the extracellular leucine-rich repeat domain of MIK2 in vivo and in vitro, indicating that MIK2 is the receptor of SCOOP peptides. Perception of SCOOP peptides induces the association of MIK2 and the coreceptors SOMATIC EMBRYOGENESIS RECEPTOR KINASE 3 (SERK3) and SERK4 and relays the signaling through the cytosolic receptor-like kinases BOTRYTIS -INDUCED KINASE 1 (BIK1) and AVRPPHB SUSCEPTIBLE1 (PBS1)-LIKE 1 (PBL1). Our study identifies a plant receptor that bears a dual role in sensing the conserved peptide motif from phytocytokines and microbial proteins via a convergent signaling relay to ensure a robust immune response. Peptide signals generated during plant microbe interactions can trigger immune responses in plants. Here the authors show that SCOOP12, a member of a family of peptides present in Brassicaceae plants, and SCOOP12-like motifs in Fusarium fungi, can trigger immune responses following perception by the MIK2 receptor kinase.

Initiation of plant immune signaling requires recognition of conserved molecular patterns from microbes and herbivores by plasma membrane-localized pattern recognition receptors. Additionally, plants produce and secrete numerous small peptide hormones, termed phytocytokines, which act as secondary danger signals to modulate immunity. In Arabidopsis, the Brassicae -specific SERINE RICH ENDOGENOUS PEPTIDE (SCOOP) family consists of 14 members that are perceived by the leucine-rich repeat receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR LIKE KINASE 2 (MIK2). Recognition of SCOOP peptides elicits generic early signaling responses but knowledge on how and if SCOOPs modulate specific downstream immune defenses is limited. We report here that depletion of MIK2 or the single PROSCOOP12 precursor results in decreased Arabidopsis resistance against the generalist herbivore Spodoptera littoralis but not the specialist Pieris brassicae. Increased performance of S. littoralis on mik2-1 and proscoop12 is accompanied by a diminished accumulation of jasmonic acid, jasmonate-isoleucine and indolic glucosinolates. Additionally, we show transcriptional activation of the PROSCOOP gene family in response to insect herbivory. Our data therefore indicate that perception of endogenous SCOOP peptides by MIK2 modulates the jasmonate pathway and thereby contributes to enhanced defense against a generalist herbivore.

Plant genomes encode hundreds of receptor kinases and peptides, but the number of known plant receptor-ligand pairs is limited. We report that the Arabidopsis leucine-rich repeat receptor kinase LRR-RK MALE DISCOVERER 1-INTERACTING RECEPTOR LIKE KINASE 2 (MIK2) is the receptor for the SERINE RICH ENDOGENOUS PEPTIDE (SCOOP) phytocytokines. MIK2 is necessary and sufficient for immune responses triggered by multiple SCOOP peptides, suggesting that MIK2 is the receptor for this divergent family of peptides. Accordingly, the SCOOP12 peptide directly binds MIK2 and triggers complex formation between MIK2 and the BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) co-receptor. MIK2 is required for resistance to the important root pathogen Fusarium oxysporum . Notably, we reveal that Fusarium proteomes encode SCOOP-like sequences, and corresponding synthetic peptides induce MIK2-dependent immune responses. These results suggest that MIK2 may recognise Fusarium -derived SCOOP-like sequences to induce immunity against Fusarium . The definition of SCOOPs as MIK2 ligands will help to unravel the multiple roles played by MIK2 during plant growth, development and stress responses. Secreted peptides and cell-surface localized receptor kinases allow plants to modify growth and development according to external cues. Here, Rhodes et al. show that the MIK2 receptor perceives the SERINE RICH ENDOGENOUS PEPTIDE (SCOOP) family of phytocytokines and is capable of recognising Fusarium -derived SCOOP-like peptides.

[...]the precise molecular mechanism underlying leaf senescence is still largely unexplored. Besides these well-established roles of phytohormones, small signaling peptides have emerged as indispensable regulators in various aspects of plant developmental and adaptive processes (Xie et al., 2022;Ji et al., 2025;Xiao et al., 2025;Zhang et al., 2025). [...]apoplast localized small signaling peptides are usually recognized by their specific membrane-bound receptors or co-receptors that usually belongs to the leucine-rich repeat receptor-like kinases (LRR-RLKs) family (Ji et al., 2025;Xiao et al., 2025;Zhang et al., 2025). Research has demonstrated that small signaling peptides from Arabidopsis thaliana such as CLAVATA3/EMBRYO-SURROUNDING REGION-RELATED (CLE) (Han et al., 2022;Zhang et al., 2022a,2022b), SERINE-RICH ENDOGENOUS PEPTIDE (SCOOPs) (Zhang et al., 2024a), PHYTOSULFOKINE (PSK) (Yamakawa et al., 1999;Matsubayashi et al., 2006;Komori et al., 2009), and INFLORESCENCE DEFICIENT IN ABSCISSION-LIKE6 (IDL6) (Guo et al., 2022) are integral in managing leaf senescence by modulating distinct signaling pathways, thereby providing novel mechanistic insights into the regulation of leaf senescence. 2 CLE peptides delay leaf senescence via ethylene and ROS pathways CLE proteins generally possess an N-terminal signal sequence that guides them into the secretory pathway, a central variable domain, and one or multiple conserved CLE motifs at the C-terminus, which are typically post-translationally modified to produce functional polypeptides (Fletcher, 2020;Xie et al., 2022). The decreased ethylene level in leaves leads to the accumulation of EIN3-BINDING F-BOX (EBF) proteins, which mediate the degradation of ETHYLENE-INSENSITIVE3 (EIN3) protein via the proteasome pathway (Guo and Ecker, 2003), thereby impairing EIN3 function and ethylene responses, ultimately delaying leaf senescence (Figure 1A).

Landslide susceptibility mapping is a crucial tool for disaster prevention and management. The performance of conventional data-driven model is greatly influenced by the quality of the samples data. The random selection of negative samples results in the lack of interpretability throughout the assessment process. To address this limitation and construct a high-quality negative samples database, this study introduces a physics-informed machine learning approach, combining the random forest model with Scoops 3D, to optimize the negative samples selection strategy and assess the landslide susceptibility of the study area. The Scoops 3D is employed to determine the factor of safety value leveraging Bishop’s simplified method. Instead of conventional random selection, negative samples are extracted from the areas with a high factor of safety value. Subsequently, the results of conventional random forest model and physics-informed data-driven model are analyzed and discussed, focusing on model performance and prediction uncertainty. In comparison to conventional methods, the physics-informed model, set with a safety area threshold of 3, demonstrates a noteworthy improvement in the mean AUC value by 36.7%, coupled with a reduced prediction uncertainty. It is evident that the determination of the safety area threshold exerts an impact on both prediction uncertainty and model performance.

Plant signalling peptides are typically released from larger precursors by proteolytic cleavage to regulate plant growth, development and stress responses. Recent studies reported the characterization of a divergent family of Brassicaceae-specific peptides, SERINE RICH ENDOGENOUS PEPTIDES (SCOOPs), and their perception by the leucine-rich repeat receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2). Here, we reveal that the SCOOP family is highly expanded, containing at least 50 members in the Columbia-0 reference Arabidopsis thaliana genome. Notably, perception of these peptides is strictly MIK2-dependent. How bioactive SCOOP peptides are produced, and to what extent their perception is responsible for the multiple physiological roles associated with MIK2 are currently unclear. Using N-terminomics, we validate the N-terminal cleavage site of representative PROSCOOPs. The cleavage sites are determined by conserved motifs upstream of the minimal SCOOP bioactive epitope. We identified subtilases necessary and sufficient to process PROSCOOP peptides at conserved cleavage motifs. Mutation of these subtilases, or their recognition motifs, suppressed PROSCOOP cleavage and associated overexpression phenotypes. Furthermore, we show that higher-order mutants of these subtilases show phenotypes reminiscent of mik2 null mutant plants, consistent with impaired PROSCOOP biogenesis, and demonstrating biological relevance of SCOOP perception by MIK2. Together, this work provides insights into the molecular mechanisms underlying the functions of the recently identified SCOOP peptides and their receptor MIK2.The SCOOP signalling peptide family expands to 50 members, whose activities are strictly dependent upon the receptor kinase MIK2. Two subtilase classes process PROSCOOPs, generating bioactive SCOOP peptides. A subtilase mutant phenocopies the mik2 receptor mutant.