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Arabidopsis phytochelatin synthase 1, but not phytochelatin synthesis, functions in extracellular defense against multiple fungal pathogens

https://doi.org/10.1101/568113
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/bs.abr.2016.06.007openalex-snapshot
The Function of Glucosinolates and Related Metabolites in Plant Innate Immunity
inferredcites →https://doi.org/10.1016/j.bbamem.2015.12.021openalex-snapshot
Effects of protein crowding on membrane systems
inferredcites →https://doi.org/10.1016/j.febslet.2006.10.050openalex-snapshot
Vacuolar sequestration of glutathione S‐conjugates outcompetes a possible degradation of the glutathione moiety by phytochelatin synthase
inferredcites →https://doi.org/10.1016/j.pbi.2008.04.004openalex-snapshot
Arabidopsis non-host resistance to powdery mildews
inferredcites →https://doi.org/10.1016/j.pbi.2009.06.007openalex-snapshot
Host–pathogen warfare at the plant cell wall
inferredcites →https://doi.org/10.1016/s0031-9422(02)00565-4openalex-snapshot
Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
inferredcites →https://doi.org/10.1016/s0968-0004(01)01938-7openalex-snapshot
Macromolecular crowding: obvious but underappreciated
inferredcites →https://doi.org/10.1021/pr1009433openalex-snapshot
Analysis of theArabidopsisCytosolic Proteome Highlights Subcellular Partitioning of Central Plant Metabolism
inferredcites →https://doi.org/10.1038/nature02076openalex-snapshot
SNARE-protein-mediated disease resistance at the plant cell wall
inferredcites →https://doi.org/10.1073/pnas.0509971102openalex-snapshot
Phytochelatin synthase, papain's cousin, in stereo
inferredcites →https://doi.org/10.1073/pnas.1615625114openalex-snapshot
Biosynthesis of cabbage phytoalexins from indole glucosinolate
inferredcites →https://doi.org/10.1073/pnas.1817233116openalex-snapshot
Balancing trade-offs between biotic and abiotic stress responses through leaf age-dependent variation in stress hormone cross-talk
inferredcites →https://doi.org/10.1073/pnas.86.18.6838openalex-snapshot
Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)
inferredcites →https://doi.org/10.1073/pnas.97.7.3718openalex-snapshot
Random GFP∷cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
inferredcites →https://doi.org/10.1074/jbc.m313142200openalex-snapshot
Phytochelatin Synthase, a Dipeptidyltransferase That Undergoes Multisite Acylation with γ-Glutamylcysteine during Catalysis
inferredcites →https://doi.org/10.1093/emboj/18.12.3325openalex-snapshot
Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast
inferredcites →https://doi.org/10.1093/jxb/ern205openalex-snapshot
Focal accumulation of defences at sites of fungal pathogen attack
inferredcites →https://doi.org/10.1094/mpmi-22-8-0953openalex-snapshot
The ERECTA Receptor-Like Kinase Regulates Cell Wall–Mediated Resistance to Pathogens in Arabidopsis thaliana
inferredcites →https://doi.org/10.1104/pp.104.048579openalex-snapshot
Weeds, Worms, and More. Papain's Long-Lost Cousin, Phytochelatin Synthase
inferredcites →https://doi.org/10.1104/pp.106.082131openalex-snapshot
Mutagenic Definition of a Papain-Like Catalytic Triad, Sufficiency of the N-Terminal Domain for Single-Site Core Catalytic Enzyme Acylation, and C-Terminal Domain for Augmentative Metal Activation of a Eukaryotic Phytochelatin Synthase
inferredcites →https://doi.org/10.1104/pp.107.4.1059openalex-snapshot
Cadmium-Sensitive, cad1 Mutants of Arabidopsis thaliana Are Phytochelatin Deficient
inferredcites →https://doi.org/10.1104/pp.109.149922openalex-snapshot
Cytosolic Action of Phytochelatin Synthase
inferredcites →https://doi.org/10.1104/pp.15.00182openalex-snapshot
Mutant Allele-Specific Uncoupling of PENETRATION3 Functions Reveals Engagement of the ATP-Binding Cassette Transporter in Distinct Tryptophan Metabolic Pathways
inferredcites →https://doi.org/10.1104/pp.17.01455openalex-snapshot
Glutathione Transferase U13 Functions in Pathogen-Triggered Glucosinolate Metabolism
inferredcites →https://doi.org/10.1105/tpc.105.038372openalex-snapshot
ArabidopsisPEN3/PDR8, an ATP Binding Cassette Transporter, Contributes to Nonhost Resistance to Inappropriate Pathogens That Enter by Direct Penetration
inferredcites →https://doi.org/10.1105/tpc.15.00887openalex-snapshot
Immobilized Subpopulations of Leaf Epidermal Mitochondria Mediate PENETRATION2-Dependent Pathogen Entry Control in Arabidopsis
inferredcites →https://doi.org/10.1111/j.1365-313x.2005.02545.xopenalex-snapshot
Arabidopsis thaliana subcellular responses to compatible Erysiphe cichoracearum infections
inferredcites →https://doi.org/10.1111/j.1365-313x.2006.02993.xopenalex-snapshot
Function of phytochelatin synthase in catabolism of glutathione‐conjugates
inferredcites →https://doi.org/10.1111/j.1399-3054.2012.01571.xopenalex-snapshot
Phytochelatin synthase: of a protease a peptide polymerase made
inferredcites →https://doi.org/10.1111/pce.12534openalex-snapshot
Expression of C aenorhabditis elegans PCS in the AtPCS 1‐deficient A rabidopsis thaliana cad1‐3 mutant separates the metal tolerance and non‐host resistance functions of phytochelatin synthases
inferredcites →https://doi.org/10.1111/tpj.13448openalex-snapshot
The mitochondrial complexome of Arabidopsis thaliana
inferredcites →https://doi.org/10.1126/science.1119409openalex-snapshot
Pre- and Postinvasion Defenses Both Contribute to Nonhost Resistance in Arabidopsis
inferredcites →https://doi.org/10.1126/science.1163732openalex-snapshot
A Glucosinolate Metabolism Pathway in Living Plant Cells Mediates Broad-Spectrum Antifungal Defense
inferredcites →https://doi.org/10.1126/science.1164627openalex-snapshot
Glucosinolate Metabolites Required for an Arabidopsis Innate Immune Response
inferredcites →https://doi.org/10.1126/science.230.4726.674openalex-snapshot
Phytochelatins: The Principal Heavy-Metal Complexing Peptides of Higher Plants
inferredcites →https://doi.org/10.1146/annurev-phyto-080516-035544openalex-snapshot
Evolution of Hormone Signaling Networks in Plant Defense
inferredcites →https://doi.org/10.1146/annurev.arplant.53.100301.135154openalex-snapshot
P HYTOCHELATINS AND M ETALLOTHIONEINS : Roles in Heavy Metal Detoxification and Homeostasis
inferredcites →https://doi.org/10.3389/fpls.2018.00019openalex-snapshot
The Arabidopsis thaliana Knockout Mutant for Phytochelatin Synthase1 (cad1-3) Is Defective in Callose Deposition, Bacterial Pathogen Defense and Auxin Content, But Shows an Increased Stem Lignification
inferredcites →https://doi.org/10.3389/fpls.2018.01639openalex-snapshot
Glutathione S-Transferases in the Biosynthesis of Sulfur-Containing Secondary Metabolites in Brassicaceae Plants

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/9780470015902.a0028220openalex-snapshot
Phytochelatin Synthase
inferred← citeshttps://doi.org/10.1007/978-981-19-8853-0_2openalex-snapshot
Role of Ectomycorrhizal Fungi in Human Welfare
inferred← citeshttps://doi.org/10.1101/2020.04.26.052480openalex-snapshot
bak1-5 mutation uncouples tryptophan-dependent and independent postinvasive immune pathways triggered in Arabidopsis by multiple fungal pathogens
inferred← citeshttps://doi.org/10.1111/pce.13766openalex-snapshot
De novo indol‐3‐ylmethyl glucosinolate biosynthesis, and not long‐distance transport, contributes to defence of Arabidopsis against powdery mildew
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