{"type": "FeatureCollection", "features": [{"id": "10.1016/j.molp.2024.10.010", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:16:00Z", "type": "Journal Article", "created": "2024-10-30", "title": "SCOOP10 and SCOOP12 peptides act through MIK2 receptor-like kinase to antagonistically regulate Arabidopsis leaf senescence", "description": "Leaf senescence plays a critical role in a plant's overall reproductive success due to its involvement in nutrient remobilization and allocation. However, our current understanding of the molecular mechanisms controlling leaf senescence remains limited. In this study, we show that the receptor-like kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) functions as a negative regulator of leaf senescence. We found that the SERINE-RICH ENDOGENOUS PEPTIDE 12, previously known to physically interact with MIK2, competes with SCOOP10 to regulate MIK2-dependent leaf senescence. We observed that increased expression of SCOOP10 or the application of exogenous SCOOP10 peptides accelerated leaf senescence in a MIK2-dependent manner. Conversely, SCOOP12 acted as a suppressor of MIK2-dependent leaf senescence regulation. Biochemical assays showed that SCOOP12 enhances while SCOOP10 diminishes MIK2 phosphorylation. Thus, the SCOOP12-MIK2 module might function antagonistically on SCOOP10-MIK2 signaling at late senescing stages, allowing for fine-tuned modulation of the leaf senescence process. Our study sheds light on the complex mechanisms underlying leaf senescence and provides valuable insights into the interplay between receptors, peptides, and the regulation of plant senescence.", "keywords": ["leaf senescence", "Arabidopsis Proteins", "Arabidopsis", "Protein Serine-Threonine Kinases", "Plant Senescence", "receptor-like kinase", "Plant Leaves", "SCOOP12", "Gene Expression Regulation", " Plant", "small signaling peptides", "MIK2", "Phosphorylation", "SCOOP10", "Peptides", "Protein Kinases", "Research Article"]}, "links": [{"href": "https://doi.org/10.1016/j.molp.2024.10.010"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Molecular%20Plant", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.1016/j.molp.2024.10.010", "name": "item", "description": "10.1016/j.molp.2024.10.010", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.1016/j.molp.2024.10.010"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2024-12-01T00:00:00Z"}}, {"id": "10.1038/nature02052", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:16:44Z", "type": "Journal Article", "created": "2003-10-08", "title": "Loss Of Omi Mitochondrial Protease Activity Causes The Neuromuscular Disorder Of Mnd2 Mutant Mice", "description": "The mouse mutant mnd2 (motor neuron degeneration 2) exhibits muscle wasting, neurodegeneration, involution of the spleen and thymus, and death by 40 days of age. Degeneration of striatal neurons, with astrogliosis and microglia activation, begins at around 3 weeks of age, and other neurons are affected at later stages. Here we have identified the mnd2 mutation as the missense mutation Ser276Cys in the protease domain of the nuclear-encoded mitochondrial serine protease Omi (also known as HtrA2 or Prss25). Protease activity of Omi is greatly reduced in tissues of mnd2 mice but is restored in mice rescued by a bacterial artificial chromosome transgene containing the wild-type Omi gene. Deletion of the PDZ domain partially restores protease activity to the inactive recombinant Omi protein carrying the Ser276Cys mutation, suggesting that the mutation impairs substrate access or binding to the active site pocket. Loss of Omi protease activity increases the susceptibility of mitochondria to induction of the permeability transition, and increases the sensitivity of mouse embryonic fibroblasts to stress-induced cell death. The neurodegeneration and juvenile lethality in mnd2 mice result from this defect in mitochondrial Omi protease.", "keywords": ["Male", "0301 basic medicine", "0303 health sciences", "Binding Sites", "Cell Death", "Science", "Homozygote", "Molecular Sequence Data", "Caseins", "Chromosome Mapping", "Mice", " Transgenic", "High-Temperature Requirement A Serine Peptidase 2", "Mitochondria", "Mitochondrial Proteins", "Mice", "Mice", " Neurologic Mutants", "03 medical and health sciences", "Animals", "Humans", "Calcium", "Female", "Amino Acid Sequence", "Cells", " Cultured", "Crosses", " Genetic"]}, "links": [{"href": "https://doi.org/10.1038/nature02052"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Nature", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.1038/nature02052", "name": "item", "description": "10.1038/nature02052", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.1038/nature02052"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2003-10-01T00:00:00Z"}}, {"id": "10.1038/s41477-023-01583-x", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:16:46Z", "type": "Journal Article", "created": "2023-12-04", "title": "Subtilase-mediated biogenesis of the expanded family of SERINE RICH ENDOGENOUS PEPTIDES", "description": "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.", "keywords": ["570", "Arabidopsis Proteins", "[SDV]Life Sciences [q-bio]", "Arabidopsis", "Receptors", " Cell Surface", "580 Plants (Botany)", "[SDV] Life Sciences [q-bio]", "10126 Department of Plant and Microbial Biology", "1110 Plant Science", "Taverne", "Brassicaceae", "Serine", "Life Science", "10211 Zurich-Basel Plant Science Center", "Peptides", "Protein Kinases"]}, "links": [{"href": "https://www.nature.com/articles/s41477-023-01583-x.pdf"}, {"href": "https://hal.science/hal-04394015/file/NaturePlants_subtilase_scoop_2023_revised.pdf"}, {"href": "https://doi.org/10.1038/s41477-023-01583-x"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Nature%20Plants", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.1038/s41477-023-01583-x", "name": "item", "description": "10.1038/s41477-023-01583-x", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.1038/s41477-023-01583-x"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2023-12-04T00:00:00Z"}}, {"id": "10.1104/pp.19.00818", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:17:24Z", "type": "Journal Article", "created": "2019-09-30", "title": "SnRK2 Protein Kinases and mRNA Decapping Machinery Control Root Development and Response to Salt", "description": "SNF1-RELATED PROTEIN KINASES 2 (SnRK2) are important components of early osmotic and salt stress signaling pathways in plants. The Arabidopsis (Arabidopsis thaliana) SnRK2 family comprises the abscisic acid (ABA)-activated protein kinases SnRK2.2, SnRK2.3, SnRK2.6, SnRK2.7, and SnRK2.8, and the ABA-independent subclass 1 protein kinases SnRK2.1, SnRK2.4, SnRK2.5, SnRK2.9, and SnRK2.10. ABA-independent SnRK2s act at the posttranscriptional level via phosphorylation of VARICOSE (VCS), a member of the mRNA decapping complex, that catalyzes the first step of 5'mRNA decay. Here, we identified VCS and VARICOSE RELATED (VCR) as interactors and phosphorylation targets of SnRK2.5, SnRK2.6, and SnRK2.10. All three protein kinases phosphorylated Ser-645 and Ser-1156 of VCS, whereas SnRK2.6 and SnRK2.10 also phosphorylated VCS Ser-692 and Ser-680 of VCR. We showed that subclass 1 SnRK2s, VCS, and 5' EXORIBONUCLEASE 4 (XRN4) are involved in regulating root growth under control conditions as well as modulating root system architecture in response to salt stress. Our results suggest interesting patterns of redundancy within subclass 1 SnRK2 protein kinases, with SnRK2.1, SnRK2.5, and SnRK2.9 controlling root growth under nonstress conditions and SnRK2.4 and SnRK2.10 acting mostly in response to salinity. We propose that subclass 1 SnRK2s function in root development under salt stress by affecting the transcript levels of aquaporins, as well as CYP79B2, an enzyme involved in auxin biosynthesis.", "keywords": ["0301 basic medicine", "570", "Arabidopsis", "Protein Serine-Threonine Kinases", "03 medical and health sciences", "HYPEROSMOTIC STRESS", "Life Science", "RNA", " Messenger", "TRITICUM-AESTIVUM L.", "Phosphorylation", "DIFFERENT PHOSPHORYLATION MECHANISMS", "Plant Proteins", "580", "0303 health sciences", "IDENTIFICATION", "Arabidopsis Proteins", "Biology and Life Sciences", "ABSCISIC-ACID", "ARABIDOPSIS", "GENE", "FAMILY", "OSMOTIC STRESSES", "Exoribonucleases", "Salts", "DECAY", "Protein Kinases", "Signal Transduction"]}, "links": [{"href": "https://doi.org/10.1104/pp.19.00818"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Plant%20Physiology", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "10.1104/pp.19.00818", "name": "item", "description": "10.1104/pp.19.00818", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/10.1104/pp.19.00818"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2019-09-30T00:00:00Z"}}, {"id": "1854/LU-8632050", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:22:26Z", "type": "Journal Article", "created": "2019-09-30", "title": "SnRK2 Protein Kinases and mRNA Decapping Machinery Control Root Development and Response to Salt", "description": "SNF1-RELATED PROTEIN KINASES 2 (SnRK2) are important components of early osmotic and salt stress signaling pathways in plants. The Arabidopsis (Arabidopsis thaliana) SnRK2 family comprises the abscisic acid (ABA)-activated protein kinases SnRK2.2, SnRK2.3, SnRK2.6, SnRK2.7, and SnRK2.8, and the ABA-independent subclass 1 protein kinases SnRK2.1, SnRK2.4, SnRK2.5, SnRK2.9, and SnRK2.10. ABA-independent SnRK2s act at the posttranscriptional level via phosphorylation of VARICOSE (VCS), a member of the mRNA decapping complex, that catalyzes the first step of 5'mRNA decay. Here, we identified VCS and VARICOSE RELATED (VCR) as interactors and phosphorylation targets of SnRK2.5, SnRK2.6, and SnRK2.10. All three protein kinases phosphorylated Ser-645 and Ser-1156 of VCS, whereas SnRK2.6 and SnRK2.10 also phosphorylated VCS Ser-692 and Ser-680 of VCR. We showed that subclass 1 SnRK2s, VCS, and 5' EXORIBONUCLEASE 4 (XRN4) are involved in regulating root growth under control conditions as well as modulating root system architecture in response to salt stress. Our results suggest interesting patterns of redundancy within subclass 1 SnRK2 protein kinases, with SnRK2.1, SnRK2.5, and SnRK2.9 controlling root growth under nonstress conditions and SnRK2.4 and SnRK2.10 acting mostly in response to salinity. We propose that subclass 1 SnRK2s function in root development under salt stress by affecting the transcript levels of aquaporins, as well as CYP79B2, an enzyme involved in auxin biosynthesis.", "keywords": ["0301 basic medicine", "570", "Arabidopsis", "Protein Serine-Threonine Kinases", "03 medical and health sciences", "HYPEROSMOTIC STRESS", "Life Science", "RNA", " Messenger", "TRITICUM-AESTIVUM L.", "Phosphorylation", "DIFFERENT PHOSPHORYLATION MECHANISMS", "Plant Proteins", "580", "0303 health sciences", "IDENTIFICATION", "Arabidopsis Proteins", "Biology and Life Sciences", "ABSCISIC-ACID", "ARABIDOPSIS", "GENE", "FAMILY", "OSMOTIC STRESSES", "Exoribonucleases", "Salts", "DECAY", "Protein Kinases", "Signal Transduction"]}, "links": [{"href": "https://doi.org/1854/LU-8632050"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Plant%20Physiology", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "1854/LU-8632050", "name": "item", "description": "1854/LU-8632050", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/1854/LU-8632050"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2019-09-30T00:00:00Z"}}, {"id": "38049516", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:23:23Z", "type": "Journal Article", "created": "2023-12-04", "title": "Subtilase-mediated biogenesis of the expanded family of SERINE RICH ENDOGENOUS PEPTIDES", "description": "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.", "keywords": ["570", "Arabidopsis Proteins", "[SDV]Life Sciences [q-bio]", "Arabidopsis", "Receptors", " Cell Surface", "580 Plants (Botany)", "[SDV] Life Sciences [q-bio]", "10126 Department of Plant and Microbial Biology", "1110 Plant Science", "Taverne", "Brassicaceae", "Serine", "Life Science", "10211 Zurich-Basel Plant Science Center", "Peptides", "Protein Kinases"]}, "links": [{"href": "https://www.nature.com/articles/s41477-023-01583-x.pdf"}, {"href": "https://hal.science/hal-04394015/file/NaturePlants_subtilase_scoop_2023_revised.pdf"}, {"href": "https://doi.org/38049516"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Nature%20Plants", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "38049516", "name": "item", "description": "38049516", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/38049516"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2023-12-04T00:00:00Z"}}, {"id": "PMC11630628", "type": "Feature", "geometry": null, "properties": {"updated": "2026-09-21T16:24:39Z", "type": "Journal Article", "created": "2024-10-30", "title": "SCOOP10 and SCOOP12 peptides act through MIK2 receptor-like kinase to antagonistically regulate Arabidopsis leaf senescence", "description": "Leaf senescence plays a critical role in a plant's overall reproductive success due to its involvement in nutrient remobilization and allocation. However, our current understanding of the molecular mechanisms controlling leaf senescence remains limited. In this study, we show that the receptor-like kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) functions as a negative regulator of leaf senescence. We found that the SERINE-RICH ENDOGENOUS PEPTIDE 12, previously known to physically interact with MIK2, competes with SCOOP10 to regulate MIK2-dependent leaf senescence. We observed that increased expression of SCOOP10 or the application of exogenous SCOOP10 peptides accelerated leaf senescence in a MIK2-dependent manner. Conversely, SCOOP12 acted as a suppressor of MIK2-dependent leaf senescence regulation. Biochemical assays showed that SCOOP12 enhances while SCOOP10 diminishes MIK2 phosphorylation. Thus, the SCOOP12-MIK2 module might function antagonistically on SCOOP10-MIK2 signaling at late senescing stages, allowing for fine-tuned modulation of the leaf senescence process. Our study sheds light on the complex mechanisms underlying leaf senescence and provides valuable insights into the interplay between receptors, peptides, and the regulation of plant senescence.", "keywords": ["leaf senescence", "Arabidopsis Proteins", "Arabidopsis", "Protein Serine-Threonine Kinases", "Plant Senescence", "receptor-like kinase", "Plant Leaves", "SCOOP12", "Gene Expression Regulation", " Plant", "small signaling peptides", "MIK2", "Phosphorylation", "SCOOP10", "Peptides", "Protein Kinases", "Research Article"]}, "links": [{"href": "https://doi.org/PMC11630628"}, {"rel": "related", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/Molecular%20Plant", "name": "related record", "description": "related record", "type": "application/json"}, {"rel": "self", "type": "application/geo+json", "title": "PMC11630628", "name": "item", "description": "PMC11630628", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items/PMC11630628"}, {"rel": "collection", "type": "application/json", "title": "Collection", "name": "collection", "description": "Collection", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main"}], "time": {"date": "2024-12-01T00:00:00Z"}}], "links": [{"rel": "self", "type": "application/geo+json", "title": "This document as GeoJSON", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items?keywords=Serine&f=json", "hreflang": "en-US"}, {"rel": "alternate", "type": "text/html", "title": "This document as HTML", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items?keywords=Serine&f=html", "hreflang": "en-US"}, {"rel": "collection", "type": "application/json", "title": "Collection URL", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main", "hreflang": "en-US"}, {"type": "application/geo+json", "rel": "first", "title": "items (first)", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items?keywords=Serine&", "hreflang": "en-US"}, {"rel": "last", "type": "application/geo+json", "title": "items (last)", "href": "https://repository.soilwise-he.eu/cat/collections/metadata:main/items?keywords=Serine&offset=7", "hreflang": "en-US"}], "numberMatched": 7, "numberReturned": 7, "distributedFeatures": [], "timeStamp": "2026-09-22T10:59:47.932343Z"}