ArticleBMC plant biology2016
Altered glycosylation of exported proteins, including surface immune receptors, compromises calcium and downstream signaling responses to microbe-associated molecular patterns in Arabidopsis thaliana.
Article in BMC plant biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 56 citations in OpenAlex.
- Mysterious giants in the world of lipids: long linear isoprenoid functions in plant physiology and reproduction.Journal of experimental botany · 2026Review
- Genetic Diversity, Predictive Protein Structures, and Interaction Networks of Cysteine-Rich Receptor-Like Kinases inComputational and structural biotechnology journal · 2026Article
- Article
- Pseudomonas syringae DC3000 infection increases glucosylated N-glycans in Arabidopsis thaliana.Glycoconjugate journal · 2023Article
- Clinical Value of Glycan Changes in Cerebrospinal Fluid for Evaluation of Post-Neurosurgical Bacterial Meningitis with Hemorrhagic Stroke Patients.Diagnostics (Basel, Switzerland) · 2023Article
- Review
- ALG3 contributes to stemness and radioresistance through regulating glycosylation of TGF-β receptor II in breast cancer.Journal of experimental & clinical cancer research : CR · 2021Article
- pH effects on plant calcium fluxes: lessons from acidification-mediated calcium elevation induced by the γ-glutamyl-leucine dipeptide identified from Phytophthora infestans.Scientific reports · 2019Article
- Antagonistic bacteria disrupt calcium homeostasis and immobilize algal cells.Nature communications · 2017Article
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
backgroundCalcium, as a second messenger, transduces extracellular signals into cellular reactions. A rise in cytosolic calcium concentration is one of the first plant responses after exposure to microbe-associated molecular patterns (MAMPs). We reported previously the isolation of Arabidopsis thaliana mutants with a "changed calcium elevation" (cce) response to flg22, a 22-amino-acid MAMP derived from bacterial flagellin.
resultsHere, we characterized the cce2 mutant and its weaker allelic mutant, cce3. Besides flg22, the mutants respond with a reduced calcium elevation to several other MAMPs and a plant endogenous peptide that is proteolytically processed from pre-pro-proteins during wounding. Downstream defense-related events such flg22-induced mitogen-activated protein kinase activation, accumulation of reactive oxygen species and growth arrest are also attenuated in cce2/cce3. By genetic mapping, next-generation sequencing and allelism assay, CCE2/CCE3 was identified to be ALG3 (Asparagine-linked glycosylation 3). This encodes the α-1,3-mannosyltransferase responsible for the first step of core oligosaccharide Glc3Man9GlcNAc2 glycan assembly on the endoplasmic reticulum (ER) luminal side. Complementation assays and glycan analysis in yeast alg3 mutant confirmed the reduced enzymatic function of the proteins encoded by the cce2/cce3 alleles - leading to accumulation of M5(ER), the immature five mannose-containing oligosaccharide structure found in the ER. Proper protein glycosylation is required for ER/Golgi processing and trafficking of membrane proteins to the plasma membrane. Endoglycosidase H-insensitivity of flg22 receptor, FLS2, in the cce2/cce3 mutants suggests altered glycan structures in the receptor.
conclusionProper glycosylation of MAMP receptors (or other exported proteins) is required for optimal responses to MAMPs and is important for immune signaling of host plants.
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