The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1

Cao, Yangrong; Liang, Yan; Tanaka, Kiwamu; Nguyen, Cuong T.; Jedrzejczak, R.; Joachimiak, A.; Stacey, Gary

doi:10.7554/elife.03766

Cited by 522 publications

(668 citation statements)

References 67 publications

(131 reference statements)

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“…Chitin-induced AtCERK1 homodimerisation has been proved to be necessary for its activation (Liu et al 2012). The chitin-induced signalling in Arabidopsis also required two other LysM-RLKs, named AtLYK4 and AtLYK5 (Wan et al 2012; Cao et al 2014). AtLYK5 shared overlapping function with AtLYK4 and interacted with AtCERK1 in a chitin-dependent manner.…”

Section: Resistance and Signalling In Plantsmentioning

confidence: 99%

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Chitin and chitin-related compounds in plant–fungal interactions

Pusztahelyi

2018

Mycology

153

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Chitin is the second abundant polysaccharide in the world after cellulose. It is a vital structural component of the fungal cell wall but not for plants. In plants, fungi are recognised through the perception of conserved microbe-associated molecular patterns (MAMPs) to induce MAMP-triggered immunity (MTI). Chitin polymers and their modified form, chitosan, induce host defence responses in both monocotyledons and dicotyledons. The plants’ response to chitin, chitosan, and derived oligosaccharides depends on the acetylation degree of these compounds which indicates possible biocontrol regulation of plant immune system. There has also been a considerable amount of recent research aimed at elucidating the roles of chitin hydrolases in fungi and plants as chitinase production in plants is not considered solely as an antifungal resistance mechanism. We discuss the importance of chitin forms and chitinases in the plant–fungal interactions and their role in persistent and possible biocontrol.Abbreviations ET, ethylene; GAP, GTPase-activating protein; GEF, GDP/GTP exchange factor; JA, jasmonic acid; LysM, lysin motif; MAMP, microbe-associated molecular pattern; MTI, MAMP-triggered immunity; NBS, nucleotide-binding site; NBS-LRR, nucleotide-binding site leucine-rich repeats; PM, powdery mildew; PR, pathogenesis-related; RBOH, respiratory burst oxidase homolog; RLK, receptor-like kinase; RLP, receptor-like protein; SA, salicylic acid; TF, transcription factor.

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Section: Resistance and Signalling In Plantsmentioning

confidence: 99%

“…AtLYK5 shared overlapping function with AtLYK4 and interacted with AtCERK1 in a chitin-dependent manner. Mutations in AtLYK5 resulted in a significant reduction in the plant chitin response (Cao et al 2014). …”

Section: Resistance and Signalling In Plantsmentioning

confidence: 99%

Chitin and chitin-related compounds in plant–fungal interactions

Pusztahelyi

2018

Mycology

153

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“…For example, the LysM-RLK chitin elicitor receptor kinase 1 of A. thaliana (AtCERK1) interacts with other receptor proteins to mediate responses to different signals. This protein can bind chitooligosaccharides (COs) [4], but it also interacts with two CO-binding LysM-RLKs with dead kinase domains (AtLYK5/ AtLYK4) [5] and with two peptidoglycan-binding LysM receptor-like proteins (AtLYM1/AtLYM3) [6] to mediate defense responses to these GlcNAc-containing signals. In contrast, OsCERK1 from rice …”

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confidence: 99%

LYR3, a high‐affinity LCO‐binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor

et al. 2016

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Edited by Julian Schroeder LYR3, LYK3, and NFP are lysin motif-containing receptor-like kinases (LysM-RLKs) from Medicago truncatula, involved in perception of symbiotic lipo-chitooligosaccharide (LCO) signals. Here, we show that LYR3, a highaffinity LCO-binding protein, physically interacts with LYK3, a key player regulating symbiotic interactions. In vitro, LYR3 is phosphorylated by the active kinase domain of LYK3. Fluorescence lifetime imaging/F€ orster resonance energy transfer (FLIM/FRET) experiments in tobacco protoplasts show that the interaction between LYR3 and LYK3 at the plasma membrane is disrupted or inhibited by addition of LCOs. Moreover, LYR3 attenuates the cell death response, provoked by coexpression of NFP and LYK3 in tobacco leaves.Keywords: FLIM/FRET; lipo-chitooligosaccharides; LysM-RLK; Medicago truncatula; membrane receptor complex; phosphoproteomics The extracellular domains of plant RLKs are built up of different protein domains which serve as sensors for endogenous and outer stimuli, as diverse as peptides, hormones, (peptido-) glycans, and (lipo-) chitooligosaccharides. Two prevalent extracellular protein domains consist of either leucine-rich repeats (LRRs) or lysin motifs (LysMs), which might interact with peptides or with N-acetyl-D-glucosamine (GlcNAc)-containing compounds, respectively [1,2].Recent advances in functional and structural analyses of plant RLKs, particularly in Arabidopsis, suggest that plant RLKs act in multimeric complexes [3]. For example, the LysM-RLK chitin elicitor receptor kinase 1 of A. thaliana (AtCERK1) interacts with other receptor proteins to mediate responses to different signals. This protein can bind chitooligosaccharides (COs) [4], but it also interacts with two CO-binding LysM-RLKs with dead kinase domains (AtLYK5/ AtLYK4) [5] and with two peptidoglycan-binding LysM receptor-like proteins (AtLYM1/AtLYM3) [6] to mediate defense responses to these GlcNAc-containing signals. In contrast, OsCERK1 from rice

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“…While BAK1 and other SERKs are the primary regulators downstream of FLS2 and EFR, the perception of the fungal MAMP chitin and signaling through CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) does not require BAK1 (Shan et al, 2008;Kemmerling et al, 2011;Ranf et al, 2011). Although CERK1 was considered as the major PRR for chitin (Miya et al, 2007;Wan et al, 2008Wan et al, , 2012, recent data suggest that the LYSIN MOTIF RECEPTOR KINASE5 (LYK5) is the primary receptor for chitin (Cao et al, 2014). Upon chitin elicitation, CERK1 and LYK5 form a complex to activate plant innate immunity (Cao et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…Although CERK1 was considered as the major PRR for chitin (Miya et al, 2007;Wan et al, 2008Wan et al, , 2012, recent data suggest that the LYSIN MOTIF RECEPTOR KINASE5 (LYK5) is the primary receptor for chitin (Cao et al, 2014). Upon chitin elicitation, CERK1 and LYK5 form a complex to activate plant innate immunity (Cao et al, 2014). CERK1 is also involved in the recognition of peptidoglycans (Willmann et al, 2011).…”

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confidence: 99%

Retraction

2015

The Plant Cell

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The authors of the above article request that it be retracted from The Plant Cell and issue the following statement:After publication of the article, we discovered irregularities and inappropriate data manipulation in Figure 6C produced by the first author Ching-Wei Chen from the Zimmerli laboratory. Specifically, the same blot image improperly appears twice in Figure 6, once in Figure 6A corresponding to the IP: a-GFP blot for FLS2-GFP and again in Figure 6C as IP: a-GFP for CERK1-GFP. We repeated these experiments but found that the original results associated with Figure 6C could not be replicated and instead suggest the potential for interaction between IOS1 and CERK1 in vivo in Nicotiana benthamiana. This raises questions about some of the conclusions of the article, and we feel the best course of action is to retract the article. We believe a major conclusion of the article remains unaffected, namely, that IOS1 is involved in the regulation of flg22-and elf18-triggered responses. However, we cannot rule out an additional role for IOS1 in mediating signaling by CERK1. We are undertaking follow-up experiments to verify the major findings and clarify the role of IOS1 in plant immunity signaling.www.plantcell.org/cgi/doi/10.1105/tpc.15.00374The Plant Cell, Vol. 27: 1563, May 2015 Plasma membrane-localized pattern recognition receptors (PRRs) such as FLAGELLIN SENSING2 (FLS2), EF-TU RECEPTOR (EFR), and CHITIN ELICITOR RECEPTOR KINASE1 (CERK1) recognize microbe-associated molecular patterns (MAMPs) to activate pattern-triggered immunity (PTI). A reverse genetics approach on genes responsive to the priming agent b-aminobutyric acid (BABA) revealed IMPAIRED OOMYCETE SUSCEPTIBILITY1 (IOS1) as a critical PTI player. Arabidopsis thaliana ios1 mutants were hypersusceptible to Pseudomonas syringae bacteria. Accordingly, ios1 mutants showed defective PTI responses, notably delayed upregulation of the PTI marker gene FLG22-INDUCED RECEPTOR-LIKE KINASE1, reduced callose deposition, and mitogen-activated protein kinase activation upon MAMP treatment. Moreover, Arabidopsis lines overexpressing IOS1 were more resistant to bacteria and showed a primed PTI response. In vitro pull-down, bimolecular fluorescence complementation, coimmunoprecipitation, 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 chitinmediated 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. INTRODUCTIONPlants possess multilayered recognition systems that detect pathogens at various stages of infection and proliferation. Recognition of m...

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The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1

Cited by 522 publications

References 67 publications

Chitin and chitin-related compounds in plant–fungal interactions

Chitin and chitin-related compounds in plant–fungal interactions

LYR3, a high‐affinity LCO‐binding protein of Medicago truncatula, interacts with LYK3, a key symbiotic receptor

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