Altered glycosylation of exported proteins, including surface immune receptors, compromises calcium and downstream signaling responses to microbe-associated molecular patterns in Arabidopsis thaliana
| العنوان: | Altered glycosylation of exported proteins, including surface immune receptors, compromises calcium and downstream signaling responses to microbe-associated molecular patterns in Arabidopsis thaliana |
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| المؤلفون: | Kazuhito Fujiyama, Fabian Trempel, Julia Grimmer, Justin Lee, Lore Westphal, Dierk Scheel, Stefanie Ranf, Cyril Zipfel, Hiroyuki Kajiura |
| المصدر: | BMC Plant Biology BMC plant biology, 16:31 |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | 0301 basic medicine, Glycan, Glycosylation, Arabidopsis, Receptors, Cell Surface, Plant Science, N-glycosylation, Biology, Endoplasmic Reticulum, Mannosyltransferases, 03 medical and health sciences, symbols.namesake, chemistry.chemical_compound, N-linked glycosylation, Defense, Arabidopsis thaliana, Calcium Signaling, Immune signaling, Pattern recognition receptors (PRRs), Calcium, Calcium signaling, Plant Diseases, Arabidopsis Proteins, Endoplasmic reticulum, fungi, Golgi apparatus, biology.organism_classification, Cell biology, 030104 developmental biology, chemistry, Membrane protein, Biochemistry, Mutation, symbols, biology.protein, Mitogen-Activated Protein Kinases, Flagellin, Research Article |
| الوصف: | Background Calcium, 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. Results Here, 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 M5ER, 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. Conclusion Proper glycosylation of MAMP receptors (or other exported proteins) is required for optimal responses to MAMPs and is important for immune signaling of host plants. Electronic supplementary material The online version of this article (doi:10.1186/s12870-016-0718-3) contains supplementary material, which is available to authorized users. |
| وصف الملف: | application/pdf |
| تدمد: | 1471-2229 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2ddaeaf5b08423bc0dc58970d1e96e9 https://pubmed.ncbi.nlm.nih.gov/26822404 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d2ddaeaf5b08423bc0dc58970d1e96e9 |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. | تدمد: | 14712229 |
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