Two redundant receptor-like cytoplasmic kinases function downstream of pattern recognition receptors to regulate activation of SA biosynthesis in Arabidopsis

Kong, Qing; Sun, Tongjun; Qu, Na; Ma, Junling; Li, Meng; Cheng, Yu-ti; Zhang, Qian; Wu, Di; Zhang, Zhibin; Zhang, Yuelin

doi:10.1104/pp.15.01954

Cited by 43 publications

(54 citation statements)

References 52 publications

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“…The bik1 pbl1 double mutant is normal in flg22-triggered but impaired in Peptriggered MPK activation Yamada et al, 2016a). A recent report showed that pcrk1 pcrk2 plants are slightly reduced in flg22-induced MPK activation (Kong et al, 2016). PBL27 was shown to interact with CERK1, and the pbl27 mutant was reported to exhibit impaired MPK activation in response to chitin, but elevated MPK activation in response to flg22 (Shinya et al, 2014).…”

Section: A Number Of Rlcks Have Emerged As Central Components Linkingmentioning

confidence: 99%

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Receptor Kinases in Plant-Pathogen Interactions: More Than Pattern Recognition

2017

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Section: A Number Of Rlcks Have Emerged As Central Components Linkingmentioning

confidence: 99%

“…Z. Liu et al, 2013;Shi et al, 2013;Shinya et al, 2014;Sreekanta et al, 2015;Kong et al, 2016). The rice RLCK VII members RLCK185 and RLCK176 have also been reported to mediate PGN-and chitin-induced defenses by interacting with CERK1 (Yamaguchi et al, 2013;Ao et al, 2014).…”

Section: Dynamic Control Of Prr Complexesmentioning

confidence: 99%

Receptor Kinases in Plant-Pathogen Interactions: More Than Pattern Recognition

2017

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“…Interestingly, a recent study reported that PATTERN-TRIGGERED IMMUNITY COMPROMISED RECEPTOR-LIKE CYTOPLASMIC KINASE1 (PCRK1) and PCRK2 regulate SA biosynthesis by influencing the expression of two transcription factors, SAR DEFICIENT1 (SARD1) and CALMODULIN BINDING PROTEIN 60-LIKE.g (CBP60g), in Arabidopsis (Kong et al, 2016). Moreover, in rice, PBL1 protein facilitates the activation of the SA-dependent pathway in the defense response against pathogen attack (Khare et al, 2016).…”

Section: Downstream Signal Transduction and Defense Mechanism Activatmentioning

confidence: 99%

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

et al. 2017

Plant Cell

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BROWN PLANTHOPPER RESISTANCE14 (BPH14), the first planthopper resistance gene isolated via map-based cloning in rice (Oryza sativa), encodes a coiled-coil, nucleotide binding site, leucine-rich repeat (CC-NB-LRR) protein. Several planthopper and aphid resistance genes encoding proteins with similar structures have recently been identified. Here, we analyzed the functions of the domains of BPH14 to identify molecular mechanisms underpinning BPH14-mediated planthopper resistance. The CC or NB domains alone or in combination (CC-NB [CN]) conferred a similar level of brown planthopper resistance to that of full-length (FL) BPH14. Both domains activated the salicylic acid signaling pathway and defense gene expression. In rice protoplasts and Nicotiana benthamiana leaves, these domains increased reactive oxygen species levels without triggering cell death. Additionally, the resistance domains and FL BPH14 protein formed homocomplexes that interacted with transcription factors WRKY46 and WRKY72. In rice protoplasts, the expression of FL BPH14 or its CC, NB, and CN domains increased the accumulation of WRKY46 and WRKY72 as well as WRKY46-and WRKY72-dependent transactivation activity. WRKY46 and WRKY72 bind to the promoters of the receptor-like cytoplasmic kinase gene RLCK281 and the callose synthase gene LOC_Os01g67364.1, whose transactivation activity is dependent on WRKY46 or WRKY72. These findings shed light on this important insect resistance mechanism.

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“…Notably, the cytoplasmic kinases BIK1/PBLs and BSK1 interact constitutively with FLS2 and are released upon elicitation (Lu et al, 2010a;Shi et al, 2013). Both PCRK1 and PCRK2 associate with FLS2 (Kong et al, 2016), and heterotrimeric G proteins directly interact with FLS2 to regulate PTI (Liang et al, 2016). Additionally, the DENN domain protein SCD1 that negatively regulates innate immunity associates in a ligand-independent manner with FLS2 in vivo (Korasick et al, 2010).…”

Section: Ios1 Associates With Fls2 Efr and Bak1 In A Ligand-indepenmentioning

confidence: 99%

“…Typically, the receptor-like cytoplasmic kinase BOTRYTIS-INDUCED KINASE1 (BIK1) plays a critical role in mediating early flagellin signaling from the FLS2/BAK1 receptor complex and regulates responses induced by elf18, Pep1, and chitin and thus acts as a convergent point downstream of multiple PRRs (Lu et al, 2010a;. Other receptor-like cytoplasmic kinase, such as PTI COMPRO-MISED RECEPTOR-LIKE CYTOPLASMIC KINASE1 (PCRK1) and PCRK2, function downstream of multiple PRRs (Sreekanta et al, 2015;Kong et al, 2016). In addition, BRASSINOSTEROID-SIG-NALING KINASE1 (BSK1) associates with unstimulated FLS2 (Shi et al, 2013).…”

Section: Introductionmentioning

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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Two redundant receptor-like cytoplasmic kinases function downstream of pattern recognition receptors to regulate activation of SA biosynthesis in Arabidopsis

Cited by 43 publications

References 52 publications

Receptor Kinases in Plant-Pathogen Interactions: More Than Pattern Recognition

Receptor Kinases in Plant-Pathogen Interactions: More Than Pattern Recognition

The Coiled-Coil and Nucleotide Binding Domains of BROWN PLANTHOPPER RESISTANCE14 Function in Signaling and Resistance against Planthopper in Rice

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