ArticleScientific reports2018
The tomato subtilase family includes several cell death-related proteinases with caspase specificity.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 67 citations in OpenAlex.
- The front line of defence: a meta-analysis of apoplastic proteases in plant immunity.Journal of experimental botany · 2021Pooled it
- A Peculiar Phospholipid-Binding Specificity and Cell Death-Related Properties of Tubic (International journal of molecular sciences · 2026Article
- Genome-wide identification, characterization and expression analysis of the subtilisin-like protease gene family in Quercus ilex in response to Phytophthora cinnamomi.Scientific reports · 2026Article
- Plant subtilases as key initiators of peptide ligand-receptor signaling.The Plant journal : for cell and molecular biology · 2026Review
- Plant caspase-like proteins: from function identification to application in winter rapeseed genetic breeding.Frontiers in plant science · 2026Review
- A fungal pathogen manipulates phytocytokine signaling for plant infection.Nature communications · 2025Article
- Characterization of drought-responsive subtilisin genes in upland rice: the role of OsSub14 in ABA signaling and ROS accumulation.BMC plant biology · 2025Article
- The CAPE1 peptide confers resistance against bacterial wilt in tomato.Journal of experimental botany · 2025Article
- Long-Term Phytaspase Responses inInternational journal of molecular sciences · 2025Article
- Genome-wide identification and characterization of Subtilisin-like Serine protease encoding genes in Vigna radiata L. Wilczek.Scientific reports · 2025Article
- Retrograde Transport of Tobacco Phytaspase Is Mediated by Its Partner, Tubby-like F-Box Protein 8.International journal of molecular sciences · 2025Article
- A regulatory network involving calmodulin controls phytosulfokine peptide processing during drought-induced flower abscission.The Plant cell · 2024Article
- Genome-Wide Identification, Functional Characterization, and Stress-Responsive Expression Profiling of Subtilase (International journal of molecular sciences · 2024Article
- Subtilase SBT5.2 inactivates flagellin immunogenicity in the plant apoplast.Nature communications · 2024Article
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Phytaspase Does Not Require Proteolytic Activity for Its Stress-Induced Internalization.International journal of molecular sciences · 2024Article
- Characterization of Phytaspase Proteolytic Activity Using Fluorogenic Peptide Substrates.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Subtilases: a major prospect to the genome editing in horticultural crops.Frontiers in plant science · 2024Review
- Phytaspase Is Capable of Detaching the Endoplasmic Reticulum Retrieval Signal from Tobacco Calreticulin-3.International journal of molecular sciences · 2023Article
- Ubiquitylation of PHYTOSULFOKINE RECEPTOR 1 modulates the defense response in tomato.Plant physiology · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Phytaspases are Asp-specific subtilisin-like plant proteases that have been likened to animal caspases with respect to their regulatory function in programmed cell death (PCD). We identified twelve putative phytaspase genes in tomato that differed widely in expression level and tissue-specific expression patterns. Most phytaspase genes are tandemly arranged on tomato chromosomes one, four, and eight, and many belong to taxon-specific clades, e.g. the P69 clade in the nightshade family, suggesting that these genes evolved by gene duplication after speciation. Five tomato phytaspases (SlPhyts) were expressed in N. benthamiana and purified to homogeneity. Substrate specificity was analyzed in a proteomics assay and with a panel of fluorogenic peptide substrates. Similar to animal caspases, SlPhyts recognized an extended sequence motif including Asp at the cleavage site. Clear differences in cleavage site preference were observed implying different substrates in vivo and, consequently, different physiological functions. A caspase-like function in PCD was confirmed for five of the seven tested phytaspases. Cell death was triggered by ectopic expression of SlPhyts 2, 3, 4, 5, 6 in tomato leaves by agro-infiltration, as well as in stably transformed transgenic tomato plants. SlPhyts 3, 4, and 5 were found to contribute to cell death under oxidative stress conditions.
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