The Arabidopsis Malectin-Like/LRR-RLK IOS1 Is Critical for BAK1-Dependent and BAK1-Independent Pattern-Triggered Immunity
Autor: | Dario Panzeri, Laurent Zimmerli, Yi-Chun Huang, Cyril Zipfel, Yu-Hung Yeh, Tzu-Chuan Chin, Milena Roux, Pin-Yao Huang, Yasuhiro Kadota, Hsiao-Chiao Chien, Chia-Nan Tao, Po-Wei Chu |
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Rok vydání: | 2016 |
Předmět: |
0106 biological sciences
0301 basic medicine animal diseases Mutant Arabidopsis Pseudomonas syringae chemical and pharmacologic phenomena Plant Science Protein Serine-Threonine Kinases 01 natural sciences 03 medical and health sciences Bimolecular fluorescence complementation Plant Immunity MAMP Research Articles biology Arabidopsis Proteins Aminobutyrates fungi Pattern recognition receptor Cell Biology biochemical phenomena metabolism and nutrition biology.organism_classification Elicitor Cell biology 030104 developmental biology Biochemistry biology.protein bacteria Signal transduction Mitogen-Activated Protein Kinases Protein Kinases Flagellin 010606 plant biology & botany |
Zdroj: | The Plant cell. 28(7) |
ISSN: | 1532-298X |
Popis: | Plasma membrane-localized pattern recognition receptors (PRRs) such as FLAGELLIN SENSING2 (FLS2), EF-TU RECEPTOR (EFR) and CHITIN ELICITOR RECEPTOR KINASE 1 (CERK1) recognize microbe-associated molecular patterns (MAMPs) to activate pattern-triggered immunity (PTI). A reverse genetics approach on genes responsive to the priming agent beta-aminobutyric acid (BABA) revealed IMPAIRED OOMYCETE SUSCEPTIBILITY1 (IOS1) as a critical PTI player. Arabidopsis thaliana ios1 mutants were hyper-susceptible to Pseudomonas syringae bacteria. Accordingly, ios1 mutants showed defective PTI responses, notably delayed up-regulation of the PTI-marker gene FLG22-INDUCED RECEPTOR-LIKE KINASE1 (FRK1), reduced callose deposition and mitogen-activated protein kinase activation upon MAMP treatment. Moreover, Arabidopsis lines over-expressing IOS1 were more resistant to bacteria and showed a primed PTI response. In vitro pull-down, bimolecular fluorescence complementation, co-immunoprecipitation, and mass spectrometry analyses supported the existence of complexes between the membrane-localized IOS1 and BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1 (BAK1)-dependent PRRs FLS2 and EFR, as well as with the BAK1-independent PRR CERK1. IOS1 also associated with BAK1 in a ligand-independent manner, and positively regulated FLS2-BAK1 complex formation upon MAMP treatment. In addition, IOS1 was critical for chitin-mediated PTI. Finally, ios1 mutants were defective in BABA-induced resistance and priming. This work reveals IOS1 as a novel regulatory protein of FLS2-, EFR- and CERK1-mediated signaling pathways that primes PTI activation. |
Databáze: | OpenAIRE |
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