메뉴 건너뛰기




Volumn 16, Issue 9, 2016, Pages 537-552

Regulation of pattern recognition receptor signalling in plants

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PATTERN RECOGNITION RECEPTOR; PHOSPHOTRANSFERASE;

EID: 84980316313     PISSN: 14741733     EISSN: 14741741     Source Type: Journal    
DOI: 10.1038/nri.2016.77     Document Type: Review
Times cited : (930)

References (217)
  • 1
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds, P. N. & Rathjen, J. P. Plant immunity: towards an integrated view of plant-pathogen interactions. Nat. Rev. Gen. 11, 539-548 (2010).
    • (2010) Nat. Rev. Gen. , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 2
    • 84881413993 scopus 로고    scopus 로고
    • Pivoting the plant immune system from dissection to deployment
    • Dangl, J. L., Horvath, D. M. & Staskawicz, B. J. Pivoting the plant immune system from dissection to deployment. Science 341, 746-751 (2013).
    • (2013) Science , vol.341 , pp. 746-751
    • Dangl, J.L.1    Horvath, D.M.2    Staskawicz, B.J.3
  • 3
    • 84903535147 scopus 로고    scopus 로고
    • Plant pattern-recognition receptors
    • Zipfel, C. Plant pattern-recognition receptors. Trends Immunol. 35, 345-351 (2014).
    • (2014) Trends Immunol. , vol.35 , pp. 345-351
    • Zipfel, C.1
  • 5
    • 84904888683 scopus 로고    scopus 로고
    • Receptor like proteins associate with SOBIR1-type of adaptors to form bimolecular receptor kinases
    • Gust, A. A. & Felix, G. Receptor like proteins associate with SOBIR1-type of adaptors to form bimolecular receptor kinases. Curr. Opin. Plant Biol. 21, 104-111 (2014).
    • (2014) Curr. Opin. Plant Biol. , vol.21 , pp. 104-111
    • Gust, A.A.1    Felix, G.2
  • 6
    • 84925399854 scopus 로고    scopus 로고
    • A lectin S-domain receptor kinase mediates lipopolysaccharide sensing in
    • Ranf, S. et al. A lectin S-domain receptor kinase mediates lipopolysaccharide sensing in Arabidopsis thaliana. Nat. Immunol. 16, 426-433 (2015).
    • (2015) Arabidopsis Thaliana. Nat. Immunol. , vol.16 , pp. 426-433
    • Ranf, S.1
  • 7
    • 84928897756 scopus 로고    scopus 로고
    • Effector-triggered immunity: From pathogen perception to robust defense
    • Cui, H., Tsuda, K. & Parker, J. E. Effector-triggered immunity: from pathogen perception to robust defense. Annu. Rev. Plant Biol.66, 487-511 (2015).
    • (2015) Annu. Rev. Plant Biol. , vol.66 , pp. 487-511
    • Cui, H.1    Tsuda, K.2    Parker, J.E.3
  • 8
    • 84871272212 scopus 로고    scopus 로고
    • Effector biology of plant-associated organisms: Concepts and perspectives
    • Win, J. et al. Effector biology of plant-associated organisms: concepts and perspectives. Cold Spring Harbor Symp. Quant. Biol. 77, 235-247 (2012).
    • (2012) Cold Spring Harbor Symp. Quant. Biol. , vol.77 , pp. 235-247
    • Win, J.1
  • 9
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl, J. L. & Jones, J. D. Plant pathogens and integrated defence responses to infection. Nature 411, 826-833 (2001).
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 10
    • 57749111993 scopus 로고    scopus 로고
    • From guard to decoy: A new model for perception of plant pathogen effectors
    • van der Hoorn, R. A. L. & Kamoun, S. From guard to decoy: a new model for perception of plant pathogen effectors. Plant Cell 20, 2009-2017 (2008).
    • (2008) Plant Cell , vol.20 , pp. 2009-2017
    • Van Der Hoorn, R.A.L.1    Kamoun, S.2
  • 11
    • 84912573366 scopus 로고    scopus 로고
    • A novel conserved mechanism for plant NLR protein pairs: The "integrated decoy" hypothesis
    • Cesari, S., Bernoux, M., Moncuquet, P., Kroj, T. & Dodds, P. N. A novel conserved mechanism for plant NLR protein pairs: the "integrated decoy" hypothesis. Front. Plant Sci. 5, 606 (2014).
    • (2014) Front. Plant Sci. , vol.5 , pp. 606
    • Cesari, S.1    Bernoux, M.2    Moncuquet, P.3    Kroj, T.4    Dodds, P.N.5
  • 13
    • 84958523930 scopus 로고    scopus 로고
    • Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens
    • Sarris, P. F., Cevik, V., Dagdas, G., Jones, J. D. & Krasileva, K. V. Comparative analysis of plant immune receptor architectures uncovers host proteins likely targeted by pathogens. BMC Biol. 14, 8 (2016).
    • (2016) BMC Biol. , vol.14 , pp. 8
    • Sarris, P.F.1    Cevik, V.2    Dagdas, G.3    Jones, J.D.4    Krasileva, K.V.5
  • 14
    • 84959220709 scopus 로고    scopus 로고
    • Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread
    • Kroj, T., Chanclud, E., Michel-Romiti, C., Grand, X. & Morel, J. B. Integration of decoy domains derived from protein targets of pathogen effectors into plant immune receptors is widespread. New Phytol. 210, 618-626 (2016).
    • (2016) New Phytol. , vol.210 , pp. 618-626
    • Kroj, T.1    Chanclud, E.2    Michel-Romiti, C.3    Grand, X.4    Morel, J.B.5
  • 15
    • 77956170809 scopus 로고    scopus 로고
    • RNA-based antiviral immunity
    • Ding, S. W. RNA-based antiviral immunity. Nat. Rev. Immunol. 10, 632-644 (2010).
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 632-644
    • Ding, S.W.1
  • 16
    • 84885616482 scopus 로고    scopus 로고
    • The immunity regulator BAK1 contributes to resistance against diverse RNA viruses
    • Korner, C. J. et al. The immunity regulator BAK1 contributes to resistance against diverse RNA viruses. Mol. Plant Microbe Interact. 26, 1271-1280 (2013).
    • (2013) Mol. Plant Microbe Interact. , vol.26 , pp. 1271-1280
    • Korner, C.J.1
  • 17
    • 84928777955 scopus 로고    scopus 로고
    • NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism
    • Zorzatto, C. et al. NIK1-mediated translation suppression functions as a plant antiviral immunity mechanism. Nature 520, 679-682 (2015).
    • (2015) Nature , vol.520 , pp. 679-682
    • Zorzatto, C.1
  • 18
    • 84963682471 scopus 로고    scopus 로고
    • Double-stranded RNAs induce a pattern-triggered immune signaling pathway in plants
    • Niehl, A., Wyrsch, I., Boller, T. & Heinlein, M. Double-stranded RNAs induce a pattern-triggered immune signaling pathway in plants. New Phytol. http://dx.doi.org/10.1111/nph.13944 (2016).
    • (2016) New Phytol.
    • Niehl, A.1    Wyrsch, I.2    Boller, T.3    Heinlein, M.4
  • 19
    • 84936891896 scopus 로고    scopus 로고
    • Inflammasomes: Mechanism of action, role in disease, and therapeutics
    • Guo, H., Callaway, J. B. & Ting, J. P. Inflammasomes: mechanism of action, role in disease, and therapeutics. Nat. Med. 21, 677-687 (2015).
    • (2015) Nat. Med. , vol.21 , pp. 677-687
    • Guo, H.1    Callaway, J.B.2    Ting, J.P.3
  • 20
    • 78449269327 scopus 로고    scopus 로고
    • Plant and animal sensors of conserved microbial signatures
    • Ronald, P. C. & Beutler, B. Plant and animal sensors of conserved microbial signatures. Science 330, 1061-1064 (2010).
    • (2010) Science , vol.330 , pp. 1061-1064
    • Ronald, P.C.1    Beutler, B.2
  • 21
    • 27144540463 scopus 로고    scopus 로고
    • Are innate immune signaling pathways in plants and animals conserved?
    • Ausubel, F. M. Are innate immune signaling pathways in plants and animals conserved? Nat. Immunol. 6, 973-979 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 973-979
    • Ausubel, F.M.1
  • 22
    • 80051967147 scopus 로고    scopus 로고
    • NLR functions in plant and animal immune systems: So far and yet so close
    • Maekawa, T., Kufer, T. A. & Schulze-Lefert, P. NLR functions in plant and animal immune systems: so far and yet so close. Nat. Immunol. 12, 817-826 (2011).
    • (2011) Nat. Immunol. , vol.12 , pp. 817-826
    • Maekawa, T.1    Kufer, T.A.2    Schulze-Lefert, P.3
  • 23
    • 20444493980 scopus 로고    scopus 로고
    • Plants and animals: A different taste for microbes?
    • Zipfel, C. & Felix, G. Plants and animals: a different taste for microbes? Curr. Opin. Plant Biol. 8, 353-360 (2005).
    • (2005) Curr. Opin. Plant Biol. , vol.8 , pp. 353-360
    • Zipfel, C.1    Felix, G.2
  • 24
    • 84946606600 scopus 로고    scopus 로고
    • Sensing Gram-negative bacteria: A phylogenetic perspective
    • Neyen, C. & Lemaitre, B. Sensing Gram-negative bacteria: a phylogenetic perspective. Curr. Opin. Immunol. 38, 8-17 (2016).
    • (2016) Curr. Opin. Immunol. , vol.38 , pp. 8-17
    • Neyen, C.1    Lemaitre, B.2
  • 25
    • 84952317720 scopus 로고    scopus 로고
    • And cross-regulation of pattern-recognition receptor signalling in health and disease
    • Cao, X. Self-regulation and cross-regulation of pattern-recognition receptor signalling in health and disease. Nat. Rev. Immunol. 16, 35-50 (2015).
    • (2015) Nat. Rev. Immunol. , vol.16 , pp. 35-50
    • Cao, X.1    Self-Regulation2
  • 26
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on Toll-like receptors
    • Kawai, T. & Akira, S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat. Immunol. 11, 373-384 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 27
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • O'Neill, L. A. & Bowie, A. G. The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat. Rev. Immunol. 7, 353-364 (2007).
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 28
    • 84899149746 scopus 로고    scopus 로고
    • Plant PRRs and the activation of innate immune signaling
    • Macho, A. P. & Zipfel, C. Plant PRRs and the activation of innate immune signaling. Mol. Cell 54, 263-272 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 263-272
    • Macho, A.P.1    Zipfel, C.2
  • 29
    • 0035845575 scopus 로고    scopus 로고
    • Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases
    • Shiu, S. H. & Bleecker, A. B. Receptor-like kinases from Arabidopsis form a monophyletic gene family related to animal receptor kinases. Proc. Natl Acad. Sci. USA 98, 10763-10768 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10763-10768
    • Shiu, S.H.1    Bleecker, A.B.2
  • 31
    • 34547151023 scopus 로고    scopus 로고
    • A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence
    • Chinchilla, D. et al. A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 448, 497-500 (2007).
    • (2007) Nature , vol.448 , pp. 497-500
    • Chinchilla, D.1
  • 32
    • 34547193514 scopus 로고    scopus 로고
    • The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants
    • Heese, A. et al. The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants. Proc. Natl Acad. Sci. USA 104, 12217-12222 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12217-12222
    • Heese, A.1
  • 33
    • 77951219239 scopus 로고    scopus 로고
    • Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1
    • Schulze, B. et al. Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1. J. Biol. Chem. 285, 9444-9451 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 9444-9451
    • Schulze, B.1
  • 34
    • 79960859584 scopus 로고    scopus 로고
    • The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens
    • Roux, M. et al. The Arabidopsis leucine-rich repeat receptor-like kinases BAK1/SERK3 and BKK1/SERK4 are required for innate immunity to hemibiotrophic and biotrophic pathogens. Plant Cell 23, 2440-2455 (2011).
    • (2011) Plant Cell , vol.23 , pp. 2440-2455
    • Roux, M.1
  • 35
    • 84887322156 scopus 로고    scopus 로고
    • Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex
    • Sun, Y. et al. Structural basis for flg22-induced activation of the Arabidopsis FLS2-BAK1 immune complex. Science 342, 624-628 (2013).
    • (2013) Science , vol.342 , pp. 624-628
    • Sun, Y.1
  • 36
    • 84920282062 scopus 로고    scopus 로고
    • Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1
    • Tang, J. et al. Structural basis for recognition of an endogenous peptide by the plant receptor kinase PEPR1. Cell Res. 25, 110-120 (2015).
    • (2015) Cell Res. , vol.25 , pp. 110-120
    • Tang, J.1
  • 37
    • 84938821922 scopus 로고    scopus 로고
    • Real-time dynamics of peptide ligand-dependent receptor complex formation in planta
    • Somssich, M. et al. Real-time dynamics of peptide ligand-dependent receptor complex formation in planta. Sci. Signal. 8, ra76 (2015).
    • (2015) Sci. Signal. , vol.8 , pp. ra76
    • Somssich, M.1
  • 38
    • 84860213183 scopus 로고    scopus 로고
    • Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function
    • Sun, W. et al. Probing the Arabidopsis flagellin receptor: FLS2-FLS2 association and the contributions of specific domains to signaling function. Plant Cell 24, 1096-1113 (2012).
    • (2012) Plant Cell , vol.24 , pp. 1096-1113
    • Sun, W.1
  • 39
    • 84893712288 scopus 로고    scopus 로고
    • Two for all: Receptor-associated kinases SOBIR1 and BAK1
    • Liebrand, T. W., van den Burg, H. A. & Joosten, M. H. Two for all: receptor-associated kinases SOBIR1 and BAK1. Trends Plant Sci. 19, 123-132 (2014).
    • (2014) Trends Plant Sci. , vol.19 , pp. 123-132
    • Liebrand, T.W.1    Van Den Burg, H.A.2    Joosten, M.H.3
  • 40
    • 84940899175 scopus 로고    scopus 로고
    • Changing SERKs and priorities during plant life
    • Schwessinger, B. & Rathjen, J. P. Changing SERKs and priorities during plant life. Trends Plant Sci. 20, 531-533 (2015).
    • (2015) Trends Plant Sci. , vol.20 , pp. 531-533
    • Schwessinger, B.1    Rathjen, J.P.2
  • 41
    • 84882912908 scopus 로고    scopus 로고
    • Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases
    • Santiago, J., Henzler, C. & Hothorn, M. Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases. Science 341, 889-892 (2013).
    • (2013) Science , vol.341 , pp. 889-892
    • Santiago, J.1    Henzler, C.2    Hothorn, M.3
  • 42
    • 84887215859 scopus 로고    scopus 로고
    • Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide
    • Sun, Y. et al. Structure reveals that BAK1 as a co-receptor recognizes the BRI1-bound brassinolide. Cell Res. 23, 1326-1329 (2013).
    • (2013) Cell Res. , vol.23 , pp. 1326-1329
    • Sun, Y.1
  • 43
    • 84941203044 scopus 로고    scopus 로고
    • Allosteric receptor activation by the plant peptide hormone phytosulfokine
    • Wang, J. et al. Allosteric receptor activation by the plant peptide hormone phytosulfokine. Nature 525, 265-268 (2015).
    • (2015) Nature , vol.525 , pp. 265-268
    • Wang, J.1
  • 44
    • 84942294135 scopus 로고    scopus 로고
    • Differential function of arabidopsis SERK family receptor-like kinases in stomatal patterning
    • Meng, X. et al. Differential function of arabidopsis SERK family receptor-like kinases in stomatal patterning. Curr. Biol. 25, 2361-2372 (2015).
    • (2015) Curr. Biol. , vol.25 , pp. 2361-2372
    • Meng, X.1
  • 45
    • 84958108025 scopus 로고    scopus 로고
    • Ligand-induced receptor-like kinase complex regulates floral organ abscission in arabidopsis
    • Meng, X. et al. Ligand-induced receptor-like kinase complex regulates floral organ abscission in arabidopsis. Cell Rep. 14, 1330-1338 (2016).
    • (2016) Cell Rep. , vol.14 , pp. 1330-1338
    • Meng, X.1
  • 46
    • 84969150862 scopus 로고    scopus 로고
    • Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission
    • Santiago, J. et al. Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission. eLife 5, e15075 (2016).
    • (2016) ELife , vol.5 , pp. e15075
    • Santiago, J.1
  • 47
    • 84947473426 scopus 로고    scopus 로고
    • An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity
    • Albert, I. et al. An RLP23-SOBIR1-BAK1 complex mediates NLP-triggered immunity. Nat. Plants 1, 15140 (2015).
    • (2015) Nat. Plants , vol.1 , pp. 15140
    • Albert, I.1
  • 48
    • 84954285391 scopus 로고    scopus 로고
    • Avr4 promotes Cf-4 receptor-like protein association with the BAK1/SERK3 receptor-like kinase to initiate receptor endocytosis and plant immunity
    • Postma, J. et al. Avr4 promotes Cf-4 receptor-like protein association with the BAK1/SERK3 receptor-like kinase to initiate receptor endocytosis and plant immunity. New Phytol. 210, 627-642 (2016).
    • (2016) New Phytol. , vol.210 , pp. 627-642
    • Postma, J.1
  • 49
    • 84878995857 scopus 로고    scopus 로고
    • Receptor-like kinase SOBIR1/ EVR interacts with receptor-like proteins in plant immunity against fungal infection
    • Liebrand, T. W. et al. Receptor-like kinase SOBIR1/ EVR interacts with receptor-like proteins in plant immunity against fungal infection. Proc. Natl Acad. Sci. USA 110, 10010-10015 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 10010-10015
    • Liebrand, T.W.1
  • 50
    • 84888414755 scopus 로고    scopus 로고
    • Arabidopsis receptor-like protein30 and receptor-like kinase suppressor of BIR1-1/ EVERSHED mediate innate immunity to necrotrophic fungi
    • Zhang, W. et al. Arabidopsis receptor-like protein30 and receptor-like kinase suppressor of BIR1-1/ EVERSHED mediate innate immunity to necrotrophic fungi. Plant Cell 25, 4227-4241 (2013).
    • (2013) Plant Cell , vol.25 , pp. 4227-4241
    • Zhang, W.1
  • 51
    • 84899137780 scopus 로고    scopus 로고
    • Perception of the novel MAMP eMax from different Xanthomonas species requires the Arabidopsis receptor-like protein ReMAX and the receptor kinase SOBIR
    • Jehle, A. K., Furst, U., Lipschis, M., Albert, M. & Felix, G. Perception of the novel MAMP eMax from different Xanthomonas species requires the Arabidopsis receptor-like protein ReMAX and the receptor kinase SOBIR. Plant Sign. Behav. 8, e27408 (2013).
    • (2013) Plant Sign. Behav. , vol.8 , pp. e27408
    • Jehle, A.K.1    Furst, U.2    Lipschis, M.3    Albert, M.4    Felix, G.5
  • 52
    • 84899135917 scopus 로고    scopus 로고
    • Arabidopsis thaliana receptor-like protein AtRLP23 associates with the receptor-like kinase AtSOBIR1
    • Bi, G. et al. Arabidopsis thaliana receptor-like protein AtRLP23 associates with the receptor-like kinase AtSOBIR1. Plant Sign. Behav. 9, e27937 (2014).
    • (2014) Plant Sign. Behav. , vol.9 , pp. e27937
    • Bi, G.1
  • 53
    • 84939153142 scopus 로고    scopus 로고
    • Tomato SOBIR1/EVR homologs are involved in elicitin perception and plant defense against the oomycete pathogen phytophthora parasitica
    • Peng, K. C., Wang, C. W., Wu, C. H., Huang, C. T. & Liou, R. F. Tomato SOBIR1/EVR homologs are involved in elicitin perception and plant defense against the oomycete pathogen phytophthora parasitica. Mol. Plant Microbe Interact. 28, 913-926 (2015).
    • (2015) Mol. Plant Microbe Interact. , vol.28 , pp. 913-926
    • Peng, K.C.1    Wang, C.W.2    Wu, C.H.3    Huang, C.T.4    Liou, R.F.5
  • 54
    • 84947420369 scopus 로고    scopus 로고
    • The receptor-like kinase SOBIR1 interacts with Brassica napus LepR3 and is required for Leptosphaeria maculans AvrLm1-triggered immunity
    • Ma, L. & Borhan, M. H. The receptor-like kinase SOBIR1 interacts with Brassica napus LepR3 and is required for Leptosphaeria maculans AvrLm1-triggered immunity. Front. Plant Sci. 6, 933 (2015).
    • (2015) Front. Plant Sci. , vol.6 , pp. 933
    • Ma, L.1    Borhan, M.H.2
  • 55
    • 84891804357 scopus 로고    scopus 로고
    • Fungal endopolygalacturonases are recognized as microbe-associated molecular patterns by the arabidopsis receptor-like protein RESPONSIVENESS to BOTRYTIS POLYGALACTURONASES1
    • Zhang, L. et al. Fungal endopolygalacturonases are recognized as microbe-associated molecular patterns by the arabidopsis receptor-like protein RESPONSIVENESS TO BOTRYTIS POLYGALACTURONASES1. Plant Phys. 164, 352-364 (2014).
    • (2014) Plant Phys. , vol.164 , pp. 352-364
    • Zhang, L.1
  • 56
    • 84899131887 scopus 로고    scopus 로고
    • An XA21-associated kinase (OsSERK2) regulates immunity mediated by the XA21 and XA3 immune receptors
    • Chen, X. et al. An XA21-associated kinase (OsSERK2) regulates immunity mediated by the XA21 and XA3 immune receptors. Mol. Plant 7, 874-892 (2014).
    • (2014) Mol. Plant , vol.7 , pp. 874-892
    • Chen, X.1
  • 57
    • 84981322160 scopus 로고    scopus 로고
    • The rice immune receptor XA21 recognizes a tyrosine-sulfated protein from a Gram-negative bacterium
    • Pruitt, R. N. et al. The rice immune receptor XA21 recognizes a tyrosine-sulfated protein from a Gram-negative bacterium. Sci. Adv. 1, e1500245 (2015).
    • (2015) Sci. Adv. , vol.1 , pp. e1500245
    • Pruitt, R.N.1
  • 58
    • 34250872460 scopus 로고    scopus 로고
    • BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways
    • He, K. et al. BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways. Curr. Biol. 17, 1109-1115 (2007).
    • (2007) Curr. Biol. , vol.17 , pp. 1109-1115
    • He, K.1
  • 59
    • 84955510546 scopus 로고    scopus 로고
    • Specific control of Arabidopsis BAK1/SERK4-regulated cell death by protein glycosylation
    • de Oliveira, M. V. V. et al. Specific control of Arabidopsis BAK1/SERK4-regulated cell death by protein glycosylation. Nat. Plants 2, 15218 (2016).
    • (2016) Nat. Plants , vol.2 , pp. 15218
    • De Oliveira, M.V.V.1
  • 60
    • 84963820505 scopus 로고    scopus 로고
    • Making sense of plant autoimmunity and 'negative regulators'
    • Rodriguez, E., El Ghoul, H., Mundy, J. & Petersen, M. Making sense of plant autoimmunity and 'negative regulators'. FEBS J. 283, 1385-1391 (2015).
    • (2015) FEBS J. , vol.283 , pp. 1385-1391
    • Rodriguez, E.1    El Ghoul, H.2    Mundy, J.3    Petersen, M.4
  • 61
    • 78649609189 scopus 로고    scopus 로고
    • Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice
    • Shimizu, T. et al. Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. Plant J. 64, 204-214 (2010).
    • (2010) Plant J. , vol.64 , pp. 204-214
    • Shimizu, T.1
  • 62
    • 84892922883 scopus 로고    scopus 로고
    • Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization
    • Hayafune, M. et al. Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization. Proc. Natl Acad. Sci. USA 111, E404-E413 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E404-E413
    • Hayafune, M.1
  • 63
    • 84866989809 scopus 로고    scopus 로고
    • Lysin motif-containing proteins LYP4 and LYP6 play dual roles in peptidoglycan and chitin perception in rice innate immunity
    • Liu, B. et al. Lysin motif-containing proteins LYP4 and LYP6 play dual roles in peptidoglycan and chitin perception in rice innate immunity. Plant Cell 24, 3406-3419 (2012).
    • (2012) Plant Cell , vol.24 , pp. 3406-3419
    • Liu, B.1
  • 64
    • 84916599171 scopus 로고    scopus 로고
    • OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin signaling in rice innate immunity
    • Ao, Y. et al. OsCERK1 and OsRLCK176 play important roles in peptidoglycan and chitin signaling in rice innate immunity. Plant J. 80, 1072-1084 (2014).
    • (2014) Plant J. , vol.80 , pp. 1072-1084
    • Ao, Y.1
  • 65
    • 84861665941 scopus 로고    scopus 로고
    • Chitin-induced dimerization activates a plant immune receptor
    • Liu, T. et al. Chitin-induced dimerization activates a plant immune receptor. Science 336, 1160-1164 (2012).
    • (2012) Science , vol.336 , pp. 1160-1164
    • Liu, T.1
  • 66
    • 77956550061 scopus 로고    scopus 로고
    • The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation
    • Petutschnig, E. K., Jones, A. M., Serazetdinova, L., Lipka, U. & Lipka, V. The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in Arabidopsis thaliana and subject to chitin-induced phosphorylation. J. Biol. Chem. 285, 28902-28911 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 28902-28911
    • Petutschnig, E.K.1    Jones, A.M.2    Serazetdinova, L.3    Lipka, U.4    Lipka, V.5
  • 67
    • 37649023555 scopus 로고    scopus 로고
    • CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
    • Miya, A. et al. CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc. Natl Acad. Sci. USA 104, 19613-19618 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19613-19618
    • Miya, A.1
  • 68
    • 84966391302 scopus 로고    scopus 로고
    • The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1
    • Cao, Y. et al. The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1. eLife http://dx.doi.org/10.7554/eLife.03766 (2014).
    • (2014) ELife
    • Cao, Y.1
  • 69
    • 84865837379 scopus 로고    scopus 로고
    • LYK4, a lysin motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis
    • Wan, J. et al. LYK4, a lysin motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis. Plant Phys. 160, 396-406 (2012).
    • (2012) Plant Phys. , vol.160 , pp. 396-406
    • Wan, J.1
  • 70
    • 83755195019 scopus 로고    scopus 로고
    • Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection
    • Willmann, R. et al. Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection. Proc. Natl Acad. Sci. USA 108, 19824-19829 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 19824-19829
    • Willmann, R.1
  • 71
    • 67650149299 scopus 로고    scopus 로고
    • The LysM receptor kinase CERK1 mediates bacterial perception in Arabidopsis
    • Gimenez-Ibanez, S., Ntoukakis, V. & Rathjen, J. P. The LysM receptor kinase CERK1 mediates bacterial perception in Arabidopsis. Plant Sign. Behav. 4, 539-541 (2009).
    • (2009) Plant Sign. Behav. , vol.4 , pp. 539-541
    • Gimenez-Ibanez, S.1    Ntoukakis, V.2    Rathjen, J.P.3
  • 72
    • 61449086250 scopus 로고    scopus 로고
    • AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants
    • Gimenez-Ibanez, S. et al. AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants. Curr. Biol. 19, 423-429 (2009).
    • (2009) Curr. Biol. , vol.19 , pp. 423-429
    • Gimenez-Ibanez, S.1
  • 73
    • 84878437050 scopus 로고    scopus 로고
    • LYM2-dependent chitin perception limits molecular flux via plasmodesmata
    • Faulkner, C. et al. LYM2-dependent chitin perception limits molecular flux via plasmodesmata. Proc. Natl Acad. Sci. USA 110, 9166-9170 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9166-9170
    • Faulkner, C.1
  • 74
    • 45149090440 scopus 로고    scopus 로고
    • A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis
    • Wan, J. et al. A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis. Plant Cell 20, 471-481 (2008).
    • (2008) Plant Cell , vol.20 , pp. 471-481
    • Wan, J.1
  • 75
    • 66149113974 scopus 로고    scopus 로고
    • Evolutionary history and stress regulation of plant receptor-like kinase/pelle genes
    • Lehti-Shiu, M. D., Zou, C., Hanada, K. & Shiu, S. H. Evolutionary history and stress regulation of plant receptor-like kinase/pelle genes. Plant Phys. 150, 12-26 (2009).
    • (2009) Plant Phys. , vol.150 , pp. 12-26
    • Lehti-Shiu, M.D.1    Zou, C.2    Hanada, K.3    Shiu, S.H.4
  • 76
    • 77954583000 scopus 로고    scopus 로고
    • Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector
    • Zhang, J. et al. Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector. Cell Host Microbe 7, 290-301 (2010).
    • (2010) Cell Host Microbe , vol.7 , pp. 290-301
    • Zhang, J.1
  • 77
    • 76249083550 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity
    • Lu, D. et al. A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity. Proc. Natl Acad. Sci. USA 107, 496-501 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 496-501
    • Lu, D.1
  • 78
    • 84876059178 scopus 로고    scopus 로고
    • BIK1 interacts with PEPRs to mediate ethylene-induced immunity
    • Liu, Z. et al. BIK1 interacts with PEPRs to mediate ethylene-induced immunity. Proc. Natl Acad. Sci. USA 110, 6205-6210 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6205-6210
    • Liu, Z.1
  • 79
    • 84929958928 scopus 로고    scopus 로고
    • The receptor-like cytoplasmic kinase PCRK1 contributes to pattern-triggered immunity against Pseudomonas syringae in Arabidopsis thaliana
    • Sreekanta, S. et al. The receptor-like cytoplasmic kinase PCRK1 contributes to pattern-triggered immunity against Pseudomonas syringae in Arabidopsis thaliana. New Phytol. 207, 78-90 (2015).
    • (2015) New Phytol. , vol.207 , pp. 78-90
    • Sreekanta, S.1
  • 80
    • 84875203565 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase targeted by a plant pathogen effector is directly phosphorylated by the chitin receptor and mediates rice immunity
    • Yamaguchi, K. et al. A receptor-like cytoplasmic kinase targeted by a plant pathogen effector is directly phosphorylated by the chitin receptor and mediates rice immunity. Cell Host Microbe 13, 347-357 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 347-357
    • Yamaguchi, K.1
  • 81
    • 84903178917 scopus 로고    scopus 로고
    • Selective regulation of the chitin-induced defense response by the Arabidopsis receptor-like cytoplasmic kinase PBL27
    • Shinya, T. et al. Selective regulation of the chitin-induced defense response by the Arabidopsis receptor-like cytoplasmic kinase PBL27. Plant J. 79, 56-66 (2014).
    • (2014) Plant J. , vol.79 , pp. 56-66
    • Shinya, T.1
  • 82
    • 84876760692 scopus 로고    scopus 로고
    • BR-SIGNALING KINASE1 physically associates with FLAGELLIN SENSING2 and regulates plant innate immunity in
    • Shi, H. et al. BR-SIGNALING KINASE1 physically associates with FLAGELLIN SENSING2 and regulates plant innate immunity in Arabidopsis. Plant Cell 25, 1143-1157 (2013).
    • (2013) Arabidopsis. Plant Cell , vol.25 , pp. 1143-1157
    • Shi, H.1
  • 83
    • 66249135697 scopus 로고    scopus 로고
    • A renaissance of elicitors: Perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors
    • Boller, T. & Felix, G. A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern-recognition receptors. Annu. Rev. Plant Biol. 60, 379-406 (2009).
    • (2009) Annu. Rev. Plant Biol. , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 84
    • 84911966333 scopus 로고    scopus 로고
    • Ca2+ signalling in plant immune response: From pattern recognition receptors to Ca2+ decoding mechanisms
    • Seybold, H. et al. Ca2+ signalling in plant immune response: from pattern recognition receptors to Ca2+ decoding mechanisms. New Phytol. 204, 782-790 (2014).
    • (2014) New Phytol. , vol.204 , pp. 782-790
    • Seybold, H.1
  • 86
    • 84898033684 scopus 로고    scopus 로고
    • Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity
    • Kadota, Y. et al. Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity. Mol. Cell 54, 43-55 (2014).
    • (2014) Mol. Cell , vol.54 , pp. 43-55
    • Kadota, Y.1
  • 87
    • 84896079926 scopus 로고    scopus 로고
    • The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity
    • Li, L. et al. The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity. Cell Host Microbe 15, 329-338 (2014).
    • (2014) Cell Host Microbe , vol.15 , pp. 329-338
    • Li, L.1
  • 88
    • 84949599348 scopus 로고    scopus 로고
    • PBL13 is a serine/threonine protein kinase that negatively regulates Arabidopsis immune responses
    • Lin, Z. D., Liebrand, T. W., Yadeta, K. A. & Coaker, G. L. PBL13 is a serine/threonine protein kinase that negatively regulates Arabidopsis immune responses. Plant Phys. 169, 2950-2962 (2015).
    • (2015) Plant Phys. , vol.169 , pp. 2950-2962
    • Lin, Z.D.1    Liebrand, T.W.2    Yadeta, K.A.3    Coaker, G.L.4
  • 89
    • 44049090117 scopus 로고    scopus 로고
    • Synergistic activation of the Arabidopsis NADPH oxidase AtrbohD by Ca2+ and phosphorylation
    • Ogasawara, Y. et al. Synergistic activation of the Arabidopsis NADPH oxidase AtrbohD by Ca2+ and phosphorylation. J. Biol. Chem. 283, 8885-8892 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 8885-8892
    • Ogasawara, Y.1
  • 90
    • 74049148813 scopus 로고    scopus 로고
    • Structure of the N-terminal regulatory domain of a plant NADPH oxidase and its functional implications
    • Oda, T. et al. Structure of the N-terminal regulatory domain of a plant NADPH oxidase and its functional implications. J. Biol. Chem. 285, 1435-1445 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 1435-1445
    • Oda, T.1
  • 91
    • 34250728188 scopus 로고    scopus 로고
    • Calcium-dependent protein kinases regulate the production of reactive oxygen species by potato NADPH oxidase
    • Kobayashi, M. et al. Calcium-dependent protein kinases regulate the production of reactive oxygen species by potato NADPH oxidase. Plant Cell 19, 1065-1080 (2007).
    • (2007) Plant Cell , vol.19 , pp. 1065-1080
    • Kobayashi, M.1
  • 92
    • 84878149704 scopus 로고    scopus 로고
    • Calcium-dependent protein kinase/ NADPH oxidase activation circuit is required for rapid defense signal propagation
    • Dubiella, U. et al. Calcium-dependent protein kinase/ NADPH oxidase activation circuit is required for rapid defense signal propagation. Proc. Natl Acad. Sci. USA 110, 8744-8749 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 8744-8749
    • Dubiella, U.1
  • 93
    • 77949773101 scopus 로고    scopus 로고
    • Differential innate immune signalling via Ca2+ sensor protein kinases
    • Boudsocq, M. et al. Differential innate immune signalling via Ca2+ sensor protein kinases. Nature 464, 418-422 (2010).
    • (2010) Nature , vol.464 , pp. 418-422
    • Boudsocq, M.1
  • 94
    • 84939488431 scopus 로고    scopus 로고
    • Regulation of the NADPH oxidase RBOHD during plant immunity
    • Kadota, Y., Shirasu, K. & Zipfel, C. Regulation of the NADPH oxidase RBOHD during plant immunity. Plant Cell Physiol. 56, 1472-1480 (2015).
    • (2015) Plant Cell Physiol. , vol.56 , pp. 1472-1480
    • Kadota, Y.1    Shirasu, K.2    Zipfel, C.3
  • 95
    • 84964453201 scopus 로고    scopus 로고
    • Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor
    • Liang, X. et al. Arabidopsis heterotrimeric G proteins regulate immunity by directly coupling to the FLS2 receptor. eLife 5, e13568 (2016).
    • (2016) ELife , vol.5 , pp. e13568
    • Liang, X.1
  • 96
    • 39149121438 scopus 로고    scopus 로고
    • Regulation of rice NADPH oxidase by binding of Rac GTPase to its N-terminal extension
    • Wong, H. L. et al. Regulation of rice NADPH oxidase by binding of Rac GTPase to its N-terminal extension. Plant Cell 19, 4022-4034 (2007).
    • (2007) Plant Cell , vol.19 , pp. 4022-4034
    • Wong, H.L.1
  • 97
    • 84876391971 scopus 로고    scopus 로고
    • An OsCEBiP/ OsCERK1-OsRacGEF1-OsRac1 module is an essential early component of chitin-induced rice immunity
    • Akamatsu, A. et al. An OsCEBiP/ OsCERK1-OsRacGEF1-OsRac1 module is an essential early component of chitin-induced rice immunity. Cell Host Microbe 13, 465-476 (2013).
    • (2013) Cell Host Microbe , vol.13 , pp. 465-476
    • Akamatsu, A.1
  • 98
    • 84964313705 scopus 로고    scopus 로고
    • Microbe-associated molecular pattern-induced calcium signaling requires the receptor-like cytoplasmic kinases, PBL1 and BIK1
    • Ranf, S. et al. Microbe-associated molecular pattern-induced calcium signaling requires the receptor-like cytoplasmic kinases, PBL1 and BIK1. BMC Plant Biol. 14, 374 (2014).
    • (2014) BMC Plant Biol. , vol.14 , pp. 374
    • Ranf, S.1
  • 99
    • 84944041750 scopus 로고    scopus 로고
    • The calcium-dependent protein kinase CPK28 negatively regulates the BIK1-mediated PAMP-induced calcium burst
    • Monaghan, J., Matschi, S., Romeis, T. & Zipfel, C. The calcium-dependent protein kinase CPK28 negatively regulates the BIK1-mediated PAMP-induced calcium burst. Plant Sign. Behav. 10, e1018497 (2015).
    • (2015) Plant Sign. Behav. , vol.10 , pp. e1018497
    • Monaghan, J.1    Matschi, S.2    Romeis, T.3    Zipfel, C.4
  • 100
    • 84961340608 scopus 로고    scopus 로고
    • Ethylene production in Botrytis cinerea- and oligogalacturonide-induced immunity requires calcium-dependent protein kinases
    • Gravino, M., Savatin, D. V., Macone, A. & De Lorenzo, G. Ethylene production in Botrytis cinerea- and oligogalacturonide-induced immunity requires calcium-dependent protein kinases. Plant J. 84, 1073-1086 (2015).
    • (2015) Plant J. , vol.84 , pp. 1073-1086
    • Gravino, M.1    Savatin, D.V.2    Macone, A.3    De Lorenzo, G.4
  • 101
    • 84875075249 scopus 로고    scopus 로고
    • Bifurcation of Arabidopsis NLR immune signaling via Ca2+-dependent protein kinases
    • Gao, X. et al. Bifurcation of Arabidopsis NLR immune signaling via Ca2+-dependent protein kinases. PLoS Pathog. 9, e1003127 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003127
    • Gao, X.1
  • 102
    • 0037186599 scopus 로고    scopus 로고
    • MAP kinase signalling cascade in Arabidopsis innate immunity
    • Asai, T. et al. MAP kinase signalling cascade in Arabidopsis innate immunity. Nature 415, 977-983 (2002).
    • (2002) Nature , vol.415 , pp. 977-983
    • Asai, T.1
  • 103
    • 34247254409 scopus 로고    scopus 로고
    • MEKK1 is required for flg22-induced MPK4 activation in Arabidopsis plants
    • Suarez-Rodriguez, M. C. et al. MEKK1 is required for flg22-induced MPK4 activation in Arabidopsis plants. Plant Phys. 143, 661-669 (2007).
    • (2007) Plant Phys. , vol.143 , pp. 661-669
    • Suarez-Rodriguez, M.C.1
  • 104
    • 57049183228 scopus 로고    scopus 로고
    • MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein kinase cascade to regulate innate immunity in plants
    • Gao, M. et al. MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein kinase cascade to regulate innate immunity in plants. Cell Res. 18, 1190-1198 (2008).
    • (2008) Cell Res. , vol.18 , pp. 1190-1198
    • Gao, M.1
  • 105
    • 84858982046 scopus 로고    scopus 로고
    • Activation of the Arabidopsis thaliana mitogen-activated protein kinase MPK11 by the flagellin-derived elicitor peptide, flg22
    • Bethke, G. et al. Activation of the Arabidopsis thaliana mitogen-activated protein kinase MPK11 by the flagellin-derived elicitor peptide, flg22. Mol. Plant Microbe Interact. 25, 471-480 (2012).
    • (2012) Mol. Plant Microbe Interact. , vol.25 , pp. 471-480
    • Bethke, G.1
  • 106
    • 33750557448 scopus 로고    scopus 로고
    • The Arabidopsis MAP kinase kinase MKK1 participates in defence responses to the bacterial elicitor flagellin
    • Meszaros, T. et al. The Arabidopsis MAP kinase kinase MKK1 participates in defence responses to the bacterial elicitor flagellin. Plant J. 48, 485-498 (2006).
    • (2006) Plant J. , vol.48 , pp. 485-498
    • Meszaros, T.1
  • 107
    • 17744396451 scopus 로고    scopus 로고
    • Arabidopsis map kinase 4 negatively regulates systemic acquired resistance
    • Petersen, M. et al. Arabidopsis map kinase 4 negatively regulates systemic acquired resistance. Cell 103, 1111-1120 (2000).
    • (2000) Cell , vol.103 , pp. 1111-1120
    • Petersen, M.1
  • 108
    • 84863101666 scopus 로고    scopus 로고
    • The MEKK1-MKK1/MKK2-MPK4 kinase cascade negatively regulates immunity mediated by a mitogen-activated protein kinase kinase kinase in
    • Kong, Q. et al. The MEKK1-MKK1/MKK2-MPK4 kinase cascade negatively regulates immunity mediated by a mitogen-activated protein kinase kinase kinase in Arabidopsis. Plant Cell 24, 2225-2236 (2012).
    • (2012) Arabidopsis. Plant Cell , vol.24 , pp. 2225-2236
    • Kong, Q.1
  • 109
    • 84924080788 scopus 로고    scopus 로고
    • The mRNA decay factor PAT1 functions in a pathway including MAP kinase 4 and immune receptor SUMM2
    • Roux, M. E. et al. The mRNA decay factor PAT1 functions in a pathway including MAP kinase 4 and immune receptor SUMM2. EMBO J. 34, 593-608 (2015).
    • (2015) EMBO J. , vol.34 , pp. 593-608
    • Roux, M.E.1
  • 110
    • 84863337512 scopus 로고    scopus 로고
    • Disruption of PAMP-induced MAP kinase cascade by a Pseudomonas syringae effector activates plant immunity mediated by the NB-LRR protein SUMM2
    • Zhang, Z. et al. Disruption of PAMP-induced MAP kinase cascade by a Pseudomonas syringae effector activates plant immunity mediated by the NB-LRR protein SUMM2. Cell Host Microbe 11, 253-263 (2012).
    • (2012) Cell Host Microbe , vol.11 , pp. 253-263
    • Zhang, Z.1
  • 111
    • 84912127570 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis immune-related MAPKs uncovers a role for MPK3 as negative regulator of inducible defences
    • Frei dit Frey, N. et al. Functional analysis of Arabidopsis immune-related MAPKs uncovers a role for MPK3 as negative regulator of inducible defences. Genome Biol. 15, R87 (2014).
    • (2014) Genome Biol. , vol.15 , pp. R87
    • Frei dit Frey, N.1
  • 112
    • 84870705857 scopus 로고    scopus 로고
    • Constitutively active mitogen-activated protein kinase versions reveal functions of Arabidopsis MPK4 in pathogen defense signaling
    • Berriri, S. et al. Constitutively active mitogen-activated protein kinase versions reveal functions of Arabidopsis MPK4 in pathogen defense signaling. Plant Cell 24, 4281-4293 (2012).
    • (2012) Plant Cell , vol.24 , pp. 4281-4293
    • Berriri, S.1
  • 113
    • 84860541901 scopus 로고    scopus 로고
    • Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune kinases
    • Feng, F. et al. A Xanthomonas uridine 5'-monophosphate transferase inhibits plant immune kinases. Nature 485, 114-118 (2012).
    • (2012) Nature , vol.485 , pp. 114-118
    • Feng, F.1    Et, Al.A.2
  • 114
    • 84929318318 scopus 로고    scopus 로고
    • Pathogen-secreted proteases activate a novel plant immune pathway
    • Cheng, Z. Y. et al. Pathogen-secreted proteases activate a novel plant immune pathway. Nature 521, 213-216 (2015).
    • (2015) Nature , vol.521 , pp. 213-216
    • Cheng, Z.Y.1
  • 115
    • 84879705769 scopus 로고    scopus 로고
    • MAPK cascades in plant disease resistance signaling
    • Meng, X. & Zhang, S. MAPK cascades in plant disease resistance signaling. Ann. Rev. Phytopathol. 51, 245-266 (2013).
    • (2013) Ann. Rev. Phytopathol. , vol.51 , pp. 245-266
    • Meng, X.1    Zhang, S.2
  • 117
    • 84866528957 scopus 로고    scopus 로고
    • Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways
    • Murray, P. J. & Smale, S. T. Restraint of inflammatory signaling by interdependent strata of negative regulatory pathways. Nat. Immunol. 13, 916-924 (2012).
    • (2012) Nat. Immunol. , vol.13 , pp. 916-924
    • Murray, P.J.1    Smale, S.T.2
  • 118
    • 36849029862 scopus 로고    scopus 로고
    • Signalling through kinase-defective domains: The prevalence of atypical receptor-like kinases in plants
    • Castells, E. & Casacuberta, J. M. Signalling through kinase-defective domains: the prevalence of atypical receptor-like kinases in plants. J. Exp. Bot. 58, 3503-3511 (2007).
    • (2007) J. Exp. Bot. , vol.58 , pp. 3503-3511
    • Castells, E.1    Casacuberta, J.M.2
  • 119
    • 78649642175 scopus 로고    scopus 로고
    • Pseudokinases-remnants of evolution or key allosteric regulators?
    • Zeqiraj, E. & van Aalten, D. M. F. Pseudokinases-remnants of evolution or key allosteric regulators? Curr. Opin. Struc. Biol. 20, 772-781 (2010).
    • (2010) Curr. Opin. Struc. Biol. , vol.20 , pp. 772-781
    • Zeqiraj, E.1    Van Aalten, D.M.F.2
  • 120
    • 84880549135 scopus 로고    scopus 로고
    • Receptor tyrosine kinases with intracellular pseudokinase domains
    • Mendrola, J. M., Shi, F., Park, J. H. & Lemmon, M. A. Receptor tyrosine kinases with intracellular pseudokinase domains. Biochem. Soc. Trans. 41, 1029-1036 (2013).
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1029-1036
    • Mendrola, J.M.1    Shi, F.2    Park, J.H.3    Lemmon, M.A.4
  • 123
    • 0037178785 scopus 로고    scopus 로고
    • IRAK-M is a negative regulator of Toll-like receptor signaling
    • Kobayashi, K. et al. IRAK-M is a negative regulator of Toll-like receptor signaling. Cell 110, 191-202 (2002).
    • (2002) Cell , vol.110 , pp. 191-202
    • Kobayashi, K.1
  • 124
    • 79952505326 scopus 로고    scopus 로고
    • IRAK-M regulation and function in host defense and immune homeostasis
    • Hubbard, L. L. & Moore, B. B. IRAK-M regulation and function in host defense and immune homeostasis. Infect. Dis. Rep. 2, e9 (2010).
    • (2010) Infect. Dis. Rep. , vol.2 , pp. e9
    • Hubbard, L.L.1    Moore, B.B.2
  • 125
    • 67651083654 scopus 로고    scopus 로고
    • Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis
    • Gao, M. et al. Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis. Cell Host Microbe 6, 34-44 (2009).
    • (2009) Cell Host Microbe , vol.6 , pp. 34-44
    • Gao, M.1
  • 126
    • 84892819254 scopus 로고    scopus 로고
    • The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity
    • Halter, T. et al. The leucine-rich repeat receptor kinase BIR2 is a negative regulator of BAK1 in plant immunity. Curr. Biol. 24, 134-143 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 134-143
    • Halter, T.1
  • 127
    • 84898601513 scopus 로고    scopus 로고
    • Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis
    • Blaum, B. S. et al. Structure of the pseudokinase domain of BIR2, a regulator of BAK1-mediated immune signaling in Arabidopsis. J. Struct. Biol. 186, 112-121 (2014).
    • (2014) J. Struct. Biol. , vol.186 , pp. 112-121
    • Blaum, B.S.1
  • 128
    • 0037117543 scopus 로고    scopus 로고
    • IRAK-4: A novel member of the IRAK family with the properties of an IRAK-kinase
    • Li, S. Y., Strelow, A., Fontana, E. J. & Wesche, H. IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase. Proc. Natl Acad. Sci. USA 99, 5567-5572 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5567-5572
    • Li, S.Y.1    Strelow, A.2    Fontana, E.J.3    Wesche, H.4
  • 129
    • 84907975948 scopus 로고    scopus 로고
    • IRAK4 dimerization and trans-autophosphorylation are induced by myddosome assembly
    • Ferrao, R. et al. IRAK4 dimerization and trans-autophosphorylation are induced by myddosome assembly. Mol. Cell 55, 891-903 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 891-903
    • Ferrao, R.1
  • 130
    • 84895780687 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase complex BAK1/BIK1 mediates Arabidopsis innate immunity
    • Lin, W. et al. Tyrosine phosphorylation of protein kinase complex BAK1/BIK1 mediates Arabidopsis innate immunity. Proc. Natl Acad. Sci. USA 111, 3632-3637 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 3632-3637
    • Lin, W.1
  • 131
    • 79955572402 scopus 로고    scopus 로고
    • Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1
    • Schwessinger, B. et al. Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1. PLoS Gen. 7, e1002046 (2011).
    • (2011) PLoS Gen. , vol.7 , pp. e1002046
    • Schwessinger, B.1
  • 132
    • 0028126062 scopus 로고
    • The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate
    • Felix, G., Regenass, M., Spanu, P. & Boller, T. The protein phosphatase inhibitor calyculin A mimics elicitor action in plant cells and induces rapid hyperphosphorylation of specific proteins as revealed by pulse labeling with [33P]phosphate. Proc. Natl Acad. Sci. USA 91, 952-956 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 952-956
    • Felix, G.1    Regenass, M.2    Spanu, P.3    Boller, T.4
  • 133
    • 0029010727 scopus 로고
    • Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells
    • Chandra, S. & Low, P. S. Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proc. Natl Acad. Sci. USA 92, 4120-4123 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4120-4123
    • Chandra, S.1    Low, P.S.2
  • 134
    • 54749114874 scopus 로고    scopus 로고
    • Rice XB15, a protein phosphatase 2C, negatively regulates cell death and XA21-mediated innate immunity
    • Park, C. J. et al. Rice XB15, a protein phosphatase 2C, negatively regulates cell death and XA21-mediated innate immunity. PLoS Biol. 6, e231 (2008).
    • (2008) PLoS Biol. , vol.6 , pp. e231
    • Park, C.J.1
  • 135
    • 77952396347 scopus 로고    scopus 로고
    • An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity
    • Chen, X. et al. An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity. Proc. Natl Acad. Sci. USA 107, 8029-8034 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 8029-8034
    • Chen, X.1
  • 136
    • 0035006480 scopus 로고    scopus 로고
    • Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis
    • Gomez-Gomez, L., Bauer, Z. & Boller, T. Both the extracellular leucine-rich repeat domain and the kinase activity of FSL2 are required for flagellin binding and signaling in Arabidopsis. Plant Cell 13, 1155-1163 (2001).
    • (2001) Plant Cell , vol.13 , pp. 1155-1163
    • Gomez-Gomez, L.1    Bauer, Z.2    Boller, T.3
  • 137
    • 33947198632 scopus 로고    scopus 로고
    • Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase
    • Ding, Z. et al. Phosphoprotein and phosphopeptide interactions with the FHA domain from Arabidopsis kinase-associated protein phosphatase. Biochemistry 46, 2684-2696 (2007).
    • (2007) Biochemistry , vol.46 , pp. 2684-2696
    • Ding, Z.1
  • 138
    • 84908191595 scopus 로고    scopus 로고
    • Negative control of BAK1 by protein phosphatase 2A during plant innate immunity
    • Segonzac, C. et al. Negative control of BAK1 by protein phosphatase 2A during plant innate immunity. EMBO J. 33, 2069-2079 (2014).
    • (2014) EMBO J. , vol.33 , pp. 2069-2079
    • Segonzac, C.1
  • 139
    • 84959546657 scopus 로고    scopus 로고
    • Attenuation of pattern recognition receptor signaling is mediated by a MAP kinase kinase kinase
    • Mithoe, S. C. et al. Attenuation of pattern recognition receptor signaling is mediated by a MAP kinase kinase kinase. EMBO rep. 17, 441-454 (2016).
    • (2016) EMBO Rep. , vol.17 , pp. 441-454
    • Mithoe, S.C.1
  • 140
    • 84896520139 scopus 로고    scopus 로고
    • Ubiquitin code assembly and disassembly
    • Heride, C., Urbe, S. & Clague, M. J. Ubiquitin code assembly and disassembly. Curr. Biol. 24, R215-R220 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. R215-R220
    • Heride, C.1    Urbe, S.2    Clague, M.J.3
  • 141
    • 84865298775 scopus 로고    scopus 로고
    • Dissecting negative regulation of Toll-like receptor signaling
    • Kondo, T., Kawai, T. & Akira, S. Dissecting negative regulation of Toll-like receptor signaling. Trends Immunol. 33, 449-458 (2012).
    • (2012) Trends Immunol. , vol.33 , pp. 449-458
    • Kondo, T.1    Kawai, T.2    Akira, S.3
  • 142
    • 52049119002 scopus 로고    scopus 로고
    • Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in
    • Trujillo, M., Ichimura, K., Casais, C. & Shirasu, K. Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis. Curr. Biol. 18, 1396-1401 (2008).
    • (2008) Arabidopsis. Curr. Biol. , vol.18 , pp. 1396-1401
    • Trujillo, M.1    Ichimura, K.2    Casais, C.3    Shirasu, K.4
  • 143
    • 84871857219 scopus 로고    scopus 로고
    • The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in
    • Stegmann, M. et al. The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in Arabidopsis. Plant Cell 24, 4703-4716 (2012).
    • (2012) Arabidopsis. Plant Cell , vol.24 , pp. 4703-4716
    • Stegmann, M.1
  • 144
    • 79959364526 scopus 로고    scopus 로고
    • Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity
    • Lu, D. et al. Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity. Science 332, 1439-1442 (2011).
    • (2011) Science , vol.332 , pp. 1439-1442
    • Lu, D.1
  • 145
    • 84938694398 scopus 로고    scopus 로고
    • A moving view: Subcellular trafficking processes in pattern recognition receptor-triggered plant immunity
    • Ben Khaled, S., Postma, J. & Robatzek, S. A moving view: subcellular trafficking processes in pattern recognition receptor-triggered plant immunity. Annu. Rev. Phytophatol. 53, 379-402 (2015).
    • (2015) Annu. Rev. Phytophatol. , vol.53 , pp. 379-402
    • Ben Khaled, S.1    Postma, J.2    Robatzek, S.3
  • 146
    • 84919665924 scopus 로고    scopus 로고
    • Loss of Arabidopsis thaliana Dynamin-Related Protein 2B reveals separation of innate immune signaling pathways
    • Smith, J. M. et al. Loss of Arabidopsis thaliana Dynamin-Related Protein 2B reveals separation of innate immune signaling pathways. PLoS Pathog. 10, e1004578 (2014).
    • (2014) PLoS Pathog. , vol.10 , pp. e1004578
    • Smith, J.M.1
  • 147
    • 84910642978 scopus 로고    scopus 로고
    • The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover
    • Monaghan, J. et al. The calcium-dependent protein kinase CPK28 buffers plant immunity and regulates BIK1 turnover. Cell Host Microbe 16, 605-615 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 605-615
    • Monaghan, J.1
  • 148
    • 84926522841 scopus 로고    scopus 로고
    • Transcriptional networks in plant immunity
    • Tsuda, K. & Somssich, I. E. Transcriptional networks in plant immunity. New Phytol. 206, 932-947 (2015).
    • (2015) New Phytol. , vol.206 , pp. 932-947
    • Tsuda, K.1    Somssich, I.E.2
  • 149
    • 84883199752 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in innate immunity
    • Arthur, J. S. & Ley, S. C. Mitogen-activated protein kinases in innate immunity. Nat. Rev. Immunol. 13, 679-692 (2013).
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 679-692
    • Arthur, J.S.1    Ley, S.C.2
  • 150
    • 84872818282 scopus 로고    scopus 로고
    • Dual-specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling
    • Caunt, C. J. & Keyse, S. M. Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling. FEBS J. 280, 489-504 (2013).
    • (2013) FEBS J. , vol.280 , pp. 489-504
    • Caunt, C.J.1    Keyse, S.M.2
  • 151
    • 77954288995 scopus 로고    scopus 로고
    • The Arabidopsis mitogen-activated protein kinase phosphatase PP2C5 affects seed germination, stomatal aperture, and abscisic acid-inducible gene expression
    • Brock, A. K. et al. The Arabidopsis mitogen-activated protein kinase phosphatase PP2C5 affects seed germination, stomatal aperture, and abscisic acid-inducible gene expression. Plant Phys. 153, 1098-1111 (2010).
    • (2010) Plant Phys. , vol.153 , pp. 1098-1111
    • Brock, A.K.1
  • 152
    • 80053609131 scopus 로고    scopus 로고
    • Arabidopsis MPK3 and MPK6 play different roles in basal and oligogalacturonide- or flagellin-induced resistance against Botrytis cinerea
    • Galletti, R., Ferrari, S. & De Lorenzo, G. Arabidopsis MPK3 and MPK6 play different roles in basal and oligogalacturonide- or flagellin-induced resistance against Botrytis cinerea. Plant Phys. 157, 804-814 (2011).
    • (2011) Plant Phys. , vol.157 , pp. 804-814
    • Galletti, R.1    Ferrari, S.2    De Lorenzo, G.3
  • 153
    • 34548300039 scopus 로고    scopus 로고
    • The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in
    • Schweighofer, A. et al. The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in Arabidopsis. Plant Cell 19, 2213-2224 (2007).
    • (2007) Arabidopsis. Plant Cell , vol.19 , pp. 2213-2224
    • Schweighofer, A.1
  • 154
    • 79960227966 scopus 로고    scopus 로고
    • Arabidopsis MAP Kinase Phosphatase 1 (AtMKP1) negatively regulates MPK6-mediated PAMP responses and resistance against bacteria
    • Anderson, J. C. et al. Arabidopsis MAP Kinase Phosphatase 1 (AtMKP1) negatively regulates MPK6-mediated PAMP responses and resistance against bacteria. Plant J. 67, 258-268 (2011).
    • (2011) Plant J. , vol.67 , pp. 258-268
    • Anderson, J.C.1
  • 155
    • 70849099954 scopus 로고    scopus 로고
    • MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors of salicylic acid synthesis and SNC1-mediated responses in
    • Bartels, S. et al. MAP kinase phosphatase1 and protein tyrosine phosphatase1 are repressors of salicylic acid synthesis and SNC1-mediated responses in Arabidopsis. Plant Cell 21, 2884-2897 (2009).
    • (2009) Arabidopsis. Plant Cell , vol.21 , pp. 2884-2897
    • Bartels, S.1
  • 156
    • 77956798607 scopus 로고    scopus 로고
    • MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and functionally interacts with MPK3 and MPK6
    • Lumbreras, V. et al. MAPK phosphatase MKP2 mediates disease responses in Arabidopsis and functionally interacts with MPK3 and MPK6. Plant J. 63, 1017-1030 (2010).
    • (2010) Plant J. , vol.63 , pp. 1017-1030
    • Lumbreras, V.1
  • 157
    • 49949085913 scopus 로고    scopus 로고
    • Arabidopsis MAP kinase 4 regulates gene expression through transcription factor release in the nucleus
    • Qiu, J. L. et al. Arabidopsis MAP kinase 4 regulates gene expression through transcription factor release in the nucleus. EMBO J. 27, 2214-2221 (2008).
    • (2008) EMBO J. , vol.27 , pp. 2214-2221
    • Qiu, J.L.1
  • 158
    • 79957745760 scopus 로고    scopus 로고
    • Phosphorylation of a WRKY transcription factor by two pathogen-responsive MAPKs drives phytoalexin biosynthesis in Arabidopsis
    • Mao, G. et al. Phosphorylation of a WRKY transcription factor by two pathogen-responsive MAPKs drives phytoalexin biosynthesis in Arabidopsis. Plant Cell 23, 1639-1653 (2011).
    • (2011) Plant Cell , vol.23 , pp. 1639-1653
    • Mao, G.1
  • 160
    • 84924260840 scopus 로고    scopus 로고
    • Menage a trois: The complex relationships between mitogen-activated protein kinases, WRKY transcription factors, and VQ-motif-containing proteins
    • Weyhe, M., Eschen-Lippold, L., Pecher, P., Scheel, D. & Lee, J. Menage a trois: the complex relationships between mitogen-activated protein kinases, WRKY transcription factors, and VQ-motif-containing proteins. Plant Sign. Behav. 9, e29519 (2014).
    • (2014) Plant Sign. Behav. , vol.9 , pp. e29519
    • Weyhe, M.1    Eschen-Lippold, L.2    Pecher, P.3    Scheel, D.4    Lee, J.5
  • 161
    • 84861844847 scopus 로고    scopus 로고
    • Structural and functional analysis of VQ motif-containing proteins in Arabidopsis as interacting proteins of WRKY transcription factors
    • Cheng, Y. et al. Structural and functional analysis of VQ motif-containing proteins in Arabidopsis as interacting proteins of WRKY transcription factors. Plant Phys. 159, 810-825 (2012).
    • (2012) Plant Phys. , vol.159 , pp. 810-825
    • Cheng, Y.1
  • 162
    • 84902547420 scopus 로고    scopus 로고
    • The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses
    • Pecher, P. et al. The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6 target a subclass of 'VQ-motif'-containing proteins to regulate immune responses. New Phytol. 203, 592-606 (2014).
    • (2014) New Phytol. , vol.203 , pp. 592-606
    • Pecher, P.1
  • 163
    • 82755174066 scopus 로고    scopus 로고
    • Arabidopsis sigma factor binding proteins are activators of the WRKY33 transcription factor in plant defense
    • Lai, Z. et al. Arabidopsis sigma factor binding proteins are activators of the WRKY33 transcription factor in plant defense. Plant Cell 23, 3824-3841 (2011).
    • (2011) Plant Cell , vol.23 , pp. 3824-3841
    • Lai, Z.1
  • 164
    • 84927782512 scopus 로고    scopus 로고
    • Phosphorylation of trihelix transcriptional repressor ASR3 by MAP KINASE4 negatively regulates Arabidopsis immunity
    • Li, B. et al. Phosphorylation of trihelix transcriptional repressor ASR3 by MAP KINASE4 negatively regulates Arabidopsis immunity. Plant Cell 27, 839-856 (2015).
    • (2015) Plant Cell , vol.27 , pp. 839-856
    • Li, B.1
  • 165
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD Cycle
    • Buratowski, S. Progression through the RNA polymerase II CTD Cycle. Mol. Cell 36, 541-546 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 166
    • 84920599617 scopus 로고    scopus 로고
    • Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity
    • Li, F. et al. Modulation of RNA polymerase II phosphorylation downstream of pathogen perception orchestrates plant immunity. Cell Host Microbe 16, 748-758 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 748-758
    • Li, F.1
  • 167
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson, B. A. & Kraus, W. L. New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat. Rev. Mol. Cell. Biol. 13, 411-424 (2012).
    • (2012) Nat. Rev. Mol. Cell. Biol. , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 168
    • 84930797620 scopus 로고    scopus 로고
    • PARP2 is the predominant poly(ADP-ribose) polymerase in Arabidopsis DNA damage and immune responses
    • Song, J., Keppler, B. D., Wise, R. R. & Bent, A. F. PARP2 is the predominant poly(ADP-ribose) polymerase in Arabidopsis DNA damage and immune responses. PLoS Gen. 11, e1005200 (2015).
    • (2015) PLoS Gen. , vol.11 , pp. e1005200
    • Song, J.1    Keppler, B.D.2    Wise, R.R.3    Bent, A.F.4
  • 169
    • 84924368861 scopus 로고    scopus 로고
    • Protein poly(ADP-ribosyl)ation regulates Arabidopsis immune gene expression and defense responses
    • Feng, B. et al. Protein poly(ADP-ribosyl)ation regulates Arabidopsis immune gene expression and defense responses. PLoS Gen. 11, e1004936 (2015).
    • (2015) PLoS Gen. , vol.11 , pp. e1004936
    • Feng, B.1
  • 171
    • 84897779316 scopus 로고    scopus 로고
    • The activated SA and JA signaling pathways have an influence on flg22-triggered oxidative burst and callose deposition
    • Yi, S. Y., Shirasu, K., Moon, J. S., Lee, S. G. & Kwon, S. Y. The activated SA and JA signaling pathways have an influence on flg22-triggered oxidative burst and callose deposition. PloS One 9, e88951 (2014).
    • (2014) PloS One , vol.9 , pp. e88951
    • Yi, S.Y.1    Shirasu, K.2    Moon, J.S.3    Lee, S.G.4    Kwon, S.Y.5
  • 172
    • 84912059798 scopus 로고    scopus 로고
    • Salicylic acid regulates Arabidopsis microbial pattern receptor kinase levels and signaling
    • Tateda, C. et al. Salicylic acid regulates Arabidopsis microbial pattern receptor kinase levels and signaling. Plant Cell 26, 4171-4187 (2014).
    • (2014) Plant Cell , vol.26 , pp. 4171-4187
    • Tateda, C.1
  • 173
    • 84919914188 scopus 로고    scopus 로고
    • The phytotoxin coronatine is a multifunctional component of the virulence armament of Pseudomonas syringae
    • Geng, X., Jin, L., Shimada, M., Kim, M. G. & Mackey, D. The phytotoxin coronatine is a multifunctional component of the virulence armament of Pseudomonas syringae. Planta 240, 1149-1165 (2014).
    • (2014) Planta , vol.240 , pp. 1149-1165
    • Geng, X.1    Jin, L.2    Shimada, M.3    Kim, M.G.4    Mackey, D.5
  • 174
    • 77956295099 scopus 로고    scopus 로고
    • Direct transcriptional control of the Arabidopsis immune receptor FLS2 by the ethylene-dependent transcription factors EIN3 and EIL1
    • Boutrot, F. et al. Direct transcriptional control of the Arabidopsis immune receptor FLS2 by the ethylene-dependent transcription factors EIN3 and EIL1. Proc. Natl Acad. Sci. USA 107, 14502-14507 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 14502-14507
    • Boutrot, F.1
  • 175
    • 34247349556 scopus 로고    scopus 로고
    • Pathogen-associated molecular pattern recognition rather than development of tissue necrosis contributes to bacterial induction of systemic acquired resistance in
    • Mishina, T. E. & Zeier, J. Pathogen-associated molecular pattern recognition rather than development of tissue necrosis contributes to bacterial induction of systemic acquired resistance in Arabidopsis. Plant J. 50, 500-513 (2007).
    • (2007) Arabidopsis. Plant J. , vol.50 , pp. 500-513
    • Mishina, T.E.1    Zeier, J.2
  • 176
    • 0033136465 scopus 로고    scopus 로고
    • Plants have a sensitive perception system for the most conserved domain of bacterial flagellin
    • Felix, G., Duran, J. D., Volko, S. & Boller, T. Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. Plant J. 18, 265-276 (1999).
    • (1999) Plant J. , vol.18 , pp. 265-276
    • Felix, G.1    Duran, J.D.2    Volko, S.3    Boller, T.4
  • 177
    • 84875708002 scopus 로고    scopus 로고
    • The anticipation of danger: Microbe-associated molecular pattern perception enhances AtPep-triggered oxidative burst
    • Flury, P., Klauser, D., Schulze, B., Boller, T. & Bartels, S. The anticipation of danger: microbe-associated molecular pattern perception enhances AtPep-triggered oxidative burst. Plant Phys. 161, 2023-2035 (2013).
    • (2013) Plant Phys. , vol.161 , pp. 2023-2035
    • Flury, P.1    Klauser, D.2    Schulze, B.3    Boller, T.4    Bartels, S.5
  • 178
    • 84876030715 scopus 로고    scopus 로고
    • Layered pattern receptor signaling via ethylene and endogenous elicitor peptides during Arabidopsis immunity to bacterial infection
    • Tintor, N. et al. Layered pattern receptor signaling via ethylene and endogenous elicitor peptides during Arabidopsis immunity to bacterial infection. Proc. Natl Acad. Sci. USA 110, 6211-6216 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 6211-6216
    • Tintor, N.1
  • 179
    • 80051746279 scopus 로고    scopus 로고
    • Hormone crosstalk in plant disease and defense: More than just jasmonate-salicylate antagonism
    • Robert-Seilaniantz, A., Grant, M. & Jones, J. D. Hormone crosstalk in plant disease and defense: more than just jasmonate-salicylate antagonism. Annu. Rev. Phytopathol. 49, 317-343 (2011).
    • (2011) Annu. Rev. Phytopathol. , vol.49 , pp. 317-343
    • Robert-Seilaniantz, A.1    Grant, M.2    Jones, J.D.3
  • 180
    • 33645967758 scopus 로고    scopus 로고
    • A plant miRNA contributes to antibacterial resistance by repressing auxin signaling
    • Navarro, L. et al. A plant miRNA contributes to antibacterial resistance by repressing auxin signaling. Science 312, 436-439 (2006).
    • (2006) Science , vol.312 , pp. 436-439
    • Navarro, L.1
  • 181
    • 79960266065 scopus 로고    scopus 로고
    • The microRNA miR393 re-directs secondary metabolite biosynthesis away from camalexin and towards glucosinolates
    • Robert-Seilaniantz, A. et al. The microRNA miR393 re-directs secondary metabolite biosynthesis away from camalexin and towards glucosinolates. Plant J. 67, 218-231 (2011).
    • (2011) Plant J. , vol.67 , pp. 218-231
    • Robert-Seilaniantz, A.1
  • 182
    • 84905173808 scopus 로고    scopus 로고
    • Cytokinins for immunity beyond growth, galls and green islands
    • Naseem, M., Wolfling, M. & Dandekar, T. Cytokinins for immunity beyond growth, galls and green islands. Trends Plant Sci. 19, 481-484 (2014).
    • (2014) Trends Plant Sci. , vol.19 , pp. 481-484
    • Naseem, M.1    Wolfling, M.2    Dandekar, T.3
  • 183
    • 84901005318 scopus 로고    scopus 로고
    • Plant responses to Agrobacterium tumefaciens and crown gall development
    • Gohlke, J. & Deeken, R. Plant responses to Agrobacterium tumefaciens and crown gall development. Front. Plant Sci. 5, 155 (2014).
    • (2014) Front. Plant Sci. , vol.5 , pp. 155
    • Gohlke, J.1    Deeken, R.2
  • 184
    • 84890802163 scopus 로고    scopus 로고
    • The Pseudomonas type III effector HopQ1 activates cytokinin signaling and interferes with plant innate immunity
    • Hann, D. R. et al. The Pseudomonas type III effector HopQ1 activates cytokinin signaling and interferes with plant innate immunity. New Phytol. 201, 585-598 (2014).
    • (2014) New Phytol. , vol.201 , pp. 585-598
    • Hann, D.R.1
  • 185
    • 77955585761 scopus 로고    scopus 로고
    • The cytokinin-activated transcription factor ARR2 promotes plant immunity via TGA3/ NPR1-dependent salicylic acid signaling in Arabidopsis
    • Choi, J. et al. The cytokinin-activated transcription factor ARR2 promotes plant immunity via TGA3/ NPR1-dependent salicylic acid signaling in Arabidopsis. Dev. Cell 19, 284-295 (2010).
    • (2010) Dev. Cell , vol.19 , pp. 284-295
    • Choi, J.1
  • 186
    • 84856003120 scopus 로고    scopus 로고
    • Brassinosteroids inhibit pathogen-associated molecular pattern-triggered immune signaling independent of the receptor kinase BAK1
    • Albrecht, C. et al. Brassinosteroids inhibit pathogen-associated molecular pattern-triggered immune signaling independent of the receptor kinase BAK1. Proc. Natl Acad. Sci. USA 109, 303-308 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 303-308
    • Albrecht, C.1
  • 187
    • 84856009950 scopus 로고    scopus 로고
    • Brassinosteroids modulate the efficiency of plant immune responses to microbe-associated molecular patterns
    • Belkhadir, Y. et al. Brassinosteroids modulate the efficiency of plant immune responses to microbe-associated molecular patterns. Proc. Natl Acad. Sci. USA 109, 297-302 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 297-302
    • Belkhadir, Y.1
  • 188
    • 84891787185 scopus 로고    scopus 로고
    • The transcriptional regulator BZR1 mediates trade-off between plant innate immunity and growth
    • Lozano-Duran, R. et al. The transcriptional regulator BZR1 mediates trade-off between plant innate immunity and growth. eLife 2, e00983 (2013).
    • (2013) ELife , vol.2 , pp. e00983
    • Lozano-Duran, R.1
  • 189
    • 84897085282 scopus 로고    scopus 로고
    • The bHLH transcription factor HBI1 mediates the trade-off between growth and pathogen-associated molecular pattern-triggered immunity in
    • Fan, M. et al. The bHLH transcription factor HBI1 mediates the trade-off between growth and pathogen-associated molecular pattern-triggered immunity in Arabidopsis. Plant Cell 26, 828-841 (2014).
    • (2014) Arabidopsis. Plant Cell , vol.26 , pp. 828-841
    • Fan, M.1
  • 190
    • 84897600992 scopus 로고    scopus 로고
    • Antagonistic regulation of growth and immunity by the Arabidopsis basic helix-loop-helix transcription factor homolog of brassinosteroid enhanced expression2 interacting with increased leaf inclination1 binding bHLH1
    • Malinovsky, F. G. et al. Antagonistic regulation of growth and immunity by the Arabidopsis basic helix-loop-helix transcription factor homolog of brassinosteroid enhanced expression2 interacting with increased leaf inclination1 binding bHLH1. Plant Phys. 164, 1443-1455 (2014).
    • (2014) Plant Phys. , vol.164 , pp. 1443-1455
    • Malinovsky, F.G.1
  • 191
    • 84920133713 scopus 로고    scopus 로고
    • Trade-off between growth and immunity: Role of brassinosteroids
    • Lozano-Duran, R. & Zipfel, C. Trade-off between growth and immunity: role of brassinosteroids. Trends Plant Sci. 20, 12-19 (2015).
    • (2015) Trends Plant Sci. , vol.20 , pp. 12-19
    • Lozano-Duran, R.1    Zipfel, C.2
  • 193
    • 84864398678 scopus 로고    scopus 로고
    • The peptide growth factor, phytosulfokine, attenuates pattern-triggered immunity
    • Igarashi, D., Tsuda, K. & Katagiri, F. The peptide growth factor, phytosulfokine, attenuates pattern-triggered immunity. Plant J. 71, 194-204 (2012).
    • (2012) Plant J. , vol.71 , pp. 194-204
    • Igarashi, D.1    Tsuda, K.2    Katagiri, F.3
  • 194
    • 84873059402 scopus 로고    scopus 로고
    • The tyrosine-sulfated peptide receptors PSKR1 and PSY1R modify the immunity of Arabidopsis to biotrophic and necrotrophic pathogens in an antagonistic manner
    • Mosher, S. et al. The tyrosine-sulfated peptide receptors PSKR1 and PSY1R modify the immunity of Arabidopsis to biotrophic and necrotrophic pathogens in an antagonistic manner. Plant J. 73, 469-482 (2013).
    • (2013) Plant J. , vol.73 , pp. 469-482
    • Mosher, S.1
  • 195
    • 20844434815 scopus 로고    scopus 로고
    • The primary mechanism of the IL-10-regulated anti inflammatory response is to selectively inhibit transcription
    • Murray, P. J. The primary mechanism of the IL-10-regulated anti inflammatory response is to selectively inhibit transcription. Proc. Natl Acad. Sci. USA 102, 8686-8691 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8686-8691
    • Murray, P.J.1
  • 196
    • 84910667251 scopus 로고    scopus 로고
    • Targeting of plant pattern recognition receptor-triggered immunity by bacterial type-III secretion system effectors
    • Macho, A. P. & Zipfel, C. Targeting of plant pattern recognition receptor-triggered immunity by bacterial type-III secretion system effectors. Curr. Opin. Microbiol. 23, 14-22 (2015).
    • (2015) Curr. Opin. Microbiol. , vol.23 , pp. 14-22
    • Macho, A.P.1    Zipfel, C.2
  • 197
    • 46749157912 scopus 로고    scopus 로고
    • Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity
    • Shan, L. et al. Bacterial effectors target the common signaling partner BAK1 to disrupt multiple MAMP receptor-signaling complexes and impede plant immunity. Cell Host Microbe 4, 17-27 (2008).
    • (2008) Cell Host Microbe , vol.4 , pp. 17-27
    • Shan, L.1
  • 198
    • 40149083472 scopus 로고    scopus 로고
    • Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases
    • Xiang, T. et al. Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases. Curr. Biol. 18, 74-80 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 74-80
    • Xiang, T.1
  • 199
    • 84897070558 scopus 로고    scopus 로고
    • A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation
    • Macho, A. P. et al. A bacterial tyrosine phosphatase inhibits plant pattern recognition receptor activation. Science 343, 1509-1512 (2014).
    • (2014) Science , vol.343 , pp. 1509-1512
    • Macho, A.P.1
  • 200
    • 84941277332 scopus 로고    scopus 로고
    • The decoy substrate of a pathogen effector and a pseudokinase specify pathogen-induced modified-self recognition and immunity in plants
    • Wang, G. et al. The decoy substrate of a pathogen effector and a pseudokinase specify pathogen-induced modified-self recognition and immunity in plants. Cell Host Microbe 18, 285-295 (2015).
    • (2015) Cell Host Microbe , vol.18 , pp. 285-295
    • Wang, G.1
  • 201
    • 34248218612 scopus 로고    scopus 로고
    • A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity in plants
    • Zhang, J. et al. A Pseudomonas syringae effector inactivates MAPKs to suppress PAMP-induced immunity in plants. Cell Host Microbe 1, 175-185 (2007).
    • (2007) Cell Host Microbe , vol.1 , pp. 175-185
    • Zhang, J.1
  • 202
    • 77955854952 scopus 로고    scopus 로고
    • A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis mitogen-activated protein kinase kinases
    • Wang, Y. et al. A Pseudomonas syringae ADP-ribosyltransferase inhibits Arabidopsis mitogen-activated protein kinase kinases. Plant Cell 22, 2033-2044 (2010).
    • (2010) Plant Cell , vol.22 , pp. 2033-2044
    • Wang, Y.1
  • 203
    • 0042322616 scopus 로고    scopus 로고
    • Cleavage of Arabidopsis PBS1 by a bacterial type III effector
    • Shao, F. et al. Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science 301, 1230-1233 (2003).
    • (2003) Science , vol.301 , pp. 1230-1233
    • Shao, F.1
  • 204
    • 84957927597 scopus 로고    scopus 로고
    • Using decoys to expand the recognition specificity of a plant disease resistance protein
    • Kim, S. H., Qi, D., Ashfield, T., Helm, M. & Innes, R. W. Using decoys to expand the recognition specificity of a plant disease resistance protein. Science 351, 684-687 (2016).
    • (2016) Science , vol.351 , pp. 684-687
    • Kim, S.H.1    Qi, D.2    Ashfield, T.3    Helm, M.4    Innes, R.W.5
  • 205
    • 33644527550 scopus 로고    scopus 로고
    • Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity
    • Abramovitch, R. B., Janjusevic, R., Stebbins, C. E. & Martin, G. B. Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity to suppress plant cell death and immunity. Proc. Natl Acad. Sci. USA 103, 2851-2856 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2851-2856
    • Abramovitch, R.B.1    Janjusevic, R.2    Stebbins, C.E.3    Martin, G.B.4
  • 206
    • 57649100731 scopus 로고    scopus 로고
    • Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB
    • Gohre, V. et al. Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB. Curr. Biol. 18, 1824-1832 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1824-1832
    • Gohre, V.1
  • 207
    • 83655199961 scopus 로고    scopus 로고
    • A tomato LysM receptor-like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB
    • Zeng, L., Velasquez, A. C., Munkvold, K. R., Zhang, J. & Martin, G. B. A tomato LysM receptor-like kinase promotes immunity and its kinase activity is inhibited by AvrPtoB. Plant J. 69, 92-103 (2012).
    • (2012) Plant J. , vol.69 , pp. 92-103
    • Zeng, L.1    Velasquez, A.C.2    Munkvold, K.R.3    Zhang, J.4    Martin, G.B.5
  • 208
    • 83655167376 scopus 로고    scopus 로고
    • Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector
    • Cheng, W. et al. Structural analysis of Pseudomonas syringae AvrPtoB bound to host BAK1 reveals two similar kinase-interacting domains in a type III Effector. Cell Host Microbe 10, 616-626 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 616-626
    • Cheng, W.1
  • 209
    • 84938834900 scopus 로고    scopus 로고
    • An arabidopsis plasma membrane proton ATPase modulates JA signaling and is exploited by the Pseudomonas syringae effector protein AvrB for stomatal invasion
    • Zhou, Z. et al. An arabidopsis plasma membrane proton ATPase modulates JA signaling and is exploited by the Pseudomonas syringae effector protein AvrB for stomatal invasion. Plant Cell 27, 2032-2041 (2015).
    • (2015) Plant Cell , vol.27 , pp. 2032-2041
    • Zhou, Z.1
  • 210
    • 84938884589 scopus 로고    scopus 로고
    • Phosphorylation of the plant immune regulator RPM1-INTERACTING PROTEIN4 enhances plant plasma membrane H+-ATPase activity and inhibits flagellin-triggered immune responses in Arabidopsis
    • Lee, D., Bourdais, G., Yu, G., Robatzek, S. & Coaker, G. Phosphorylation of the plant immune regulator RPM1-INTERACTING PROTEIN4 enhances plant plasma membrane H+-ATPase activity and inhibits flagellin-triggered immune responses in Arabidopsis. Plant Cell 27, 2042-2056 (2015).
    • (2015) Plant Cell , vol.27 , pp. 2042-2056
    • Lee, D.1    Bourdais, G.2    Yu, G.3    Robatzek, S.4    Coaker, G.5
  • 211
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • Mackey, D., Belkhadir, Y., Alonso, J. M., Ecker, J. R. & Dangl, J. L. Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. Cell 112, 379-389 (2003).
    • (2003) Cell , vol.112 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 212
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in
    • Mackey, D., Holt, B. F., 3rd, Wiig, A. & Dangl, J. L. RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell 108, 743-754 (2002).
    • (2002) Arabidopsis. Cell , vol.108 , pp. 743-754
    • Mackey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 213
    • 10344257928 scopus 로고    scopus 로고
    • Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1
    • Belkhadir, Y., Nimchuk, Z., Hubert, D. A., Mackey, D. & Dangl, J. L. Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1. Plant Cell 16, 2822-2835 (2004).
    • (2004) Plant Cell , vol.16 , pp. 2822-2835
    • Belkhadir, Y.1    Nimchuk, Z.2    Hubert, D.A.3    Mackey, D.4    Dangl, J.L.5
  • 214
    • 84895478823 scopus 로고    scopus 로고
    • The bacterial effector HopX1 targets JAZ transcriptional repressors to activate jasmonate signaling and promote infection in Arabidopsis
    • Gimenez-Ibanez, S. et al. The bacterial effector HopX1 targets JAZ transcriptional repressors to activate jasmonate signaling and promote infection in Arabidopsis. PLoS Biol. 12, e1001792 (2014).
    • (2014) PLoS Biol. , vol.12 , pp. e1001792
    • Gimenez-Ibanez, S.1
  • 215
    • 84887266556 scopus 로고    scopus 로고
    • Bacterial effector activates jasmonate signaling by directly targeting JAZ transcriptional repressors
    • Jiang, S. et al. Bacterial effector activates jasmonate signaling by directly targeting JAZ transcriptional repressors. PLoS Pathog. 9, e1003715 (2013).
    • (2013) PLoS Pathog. , vol.9 , pp. e1003715
    • Jiang, S.1
  • 216
    • 84923845793 scopus 로고    scopus 로고
    • The phylogenetically-related pattern recognition receptors EFR and XA21 recruit similar immune signaling components in monocots and dicots
    • Holton, N., Nekrasov, V., Ronald, P. C., Zipfel, C. The phylogenetically-related pattern recognition receptors EFR and XA21 recruit similar immune signaling components in monocots and dicots.. PLoS Pathog. 11, e1004602 (2015).
    • (2015) PLoS Pathog. , vol.11 , pp. e1004602
    • Holton, N.1    Nekrasov, V.2    Ronald, P.C.3    Zipfel, C.4
  • 217
    • 84984833750 scopus 로고    scopus 로고
    • The Arabidopsis protein phosphatase PP2C38 negatively regulates the central immune kinase BIK1
    • Couto, D. et al. The Arabidopsis protein phosphatase PP2C38 negatively regulates the central immune kinase BIK1. PLoS Pathog. http://dx.doi.org/10.1371/ journal.ppat.1005811 (2016).
    • (2016) PLoS Pathog.
    • Couto, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.