메뉴 건너뛰기




Volumn 7, Issue 4, 2011, Pages

Phosphorylation-dependent differential regulation of plant growth, cell death, and innate immunity by the regulatory receptor-like kinase BAK1

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN BAK1; PROTEIN BRI1; PROTEIN EFR; PROTEIN FLS2; PROTEIN KINASE; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; BAK1 PROTEIN, ARABIDOPSIS; BRI1 PROTEIN, ARABIDOPSIS; EFR PROTEIN, ARABIDOPSIS; FLS2 PROTEIN, ARABIDOPSIS; HYBRID PROTEIN; PATTERN RECOGNITION RECEPTOR; REACTIVE OXYGEN METABOLITE; STEROID;

EID: 79955572402     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1002046     Document Type: Article
Times cited : (382)

References (75)
  • 1
    • 2442591728 scopus 로고    scopus 로고
    • Comparative analysis of the receptor-like kinase family in Arabidopsis and rice
    • Shiu SH, Karlowski WM, Pan R, Tzeng YH, Mayer KF, et al. (2004) Comparative analysis of the receptor-like kinase family in Arabidopsis and rice. Plant Cell 16: 1220-1234.
    • (2004) Plant Cell , vol.16 , pp. 1220-1234
    • Shiu, S.H.1    Karlowski, W.M.2    Pan, R.3    Tzeng, Y.H.4    Mayer, K.F.5
  • 2
    • 77952008027 scopus 로고    scopus 로고
    • Receptor-like kinase OsSIK1 improves drought and salt stress tolerance in rice (Oryza sativa) plants
    • Ouyang SQ, Liu YF, Liu P, Lei G, He SJ, et al. (2010) Receptor-like kinase OsSIK1 improves drought and salt stress tolerance in rice (Oryza sativa) plants. Plant J.
    • (2010) Plant J
    • Ouyang, S.Q.1    Liu, Y.F.2    Liu, P.3    Lei, G.4    He, S.J.5
  • 4
    • 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, (2009) 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) Annu Rev Plant Biol , vol.60 , pp. 379-406
    • Boller, T.1    Felix, G.2
  • 5
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: towards the systems level
    • Citri A, Yarden Y, (2006) EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol 7: 505-516.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 6
    • 0037429737 scopus 로고    scopus 로고
    • Epidermal growth factor receptor: mechanisms of activation and signalling
    • Jorissen RN, Walker F, Pouliot N, Garrett TP, Ward CW, et al. (2003) Epidermal growth factor receptor: mechanisms of activation and signalling. Exp Cell Res 284: 31-53.
    • (2003) Exp Cell Res , vol.284 , pp. 31-53
    • Jorissen, R.N.1    Walker, F.2    Pouliot, N.3    Garrett, T.P.4    Ward, C.W.5
  • 7
    • 33847619358 scopus 로고    scopus 로고
    • The insulin and EGF receptor structures: new insights into ligand-induced receptor activation
    • Ward CW, Lawrence MC, Streltsov VA, Adams TE, McKern NM, (2007) The insulin and EGF receptor structures: new insights into ligand-induced receptor activation. Trends Biochem Sci 32: 129-137.
    • (2007) Trends Biochem Sci , vol.32 , pp. 129-137
    • Ward, C.W.1    Lawrence, M.C.2    Streltsov, V.A.3    Adams, T.E.4    McKern, N.M.5
  • 8
    • 62649103876 scopus 로고    scopus 로고
    • The ErbB kinase domain: structural perspectives into kinase activation and inhibition
    • Bose R, Zhang X, (2009) The ErbB kinase domain: structural perspectives into kinase activation and inhibition. Exp Cell Res 315: 649-658.
    • (2009) Exp Cell Res , vol.315 , pp. 649-658
    • Bose, R.1    Zhang, X.2
  • 9
    • 67549145398 scopus 로고    scopus 로고
    • Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment
    • Jura N, Endres NF, Engel K, Deindl S, Das R, et al. (2009) Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. Cell 137: 1293-1307.
    • (2009) Cell , vol.137 , pp. 1293-1307
    • Jura, N.1    Endres, N.F.2    Engel, K.3    Deindl, S.4    Das, R.5
  • 10
    • 67449146917 scopus 로고    scopus 로고
    • The juxtamembrane region of the EGF receptor functions as an activation domain
    • Red Brewer M, Choi SH, Alvarado D, Moravcevic K, Pozzi A, et al. (2009) The juxtamembrane region of the EGF receptor functions as an activation domain. Mol Cell 34: 641-651.
    • (2009) Mol Cell , vol.34 , pp. 641-651
    • Red Brewer, M.1    Choi, S.H.2    Alvarado, D.3    Moravcevic, K.4    Pozzi, A.5
  • 11
    • 55849103180 scopus 로고    scopus 로고
    • Quantitative proteomics and phosphoproteomics reveal novel insights into complexity and dynamics of the EGFR signaling network
    • Morandell S, Stasyk T, Skvortsov S, Ascher S, Huber LA, (2008) Quantitative proteomics and phosphoproteomics reveal novel insights into complexity and dynamics of the EGFR signaling network. Proteomics 8: 4383-4401.
    • (2008) Proteomics , vol.8 , pp. 4383-4401
    • Morandell, S.1    Stasyk, T.2    Skvortsov, S.3    Ascher, S.4    Huber, L.A.5
  • 12
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson LN, Noble ME, Owen DJ, (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 13
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G, (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15: 661-675.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 15
    • 77149157499 scopus 로고    scopus 로고
    • The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity
    • Postel S, Kufner I, Beuter C, Mazzotta S, Schwedt A, et al. (2009) The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated in Arabidopsis development and immunity. Eur J Cell Biol.
    • (2009) Eur J Cell Biol
    • Postel, S.1    Kufner, I.2    Beuter, C.3    Mazzotta, S.4    Schwedt, A.5
  • 16
    • 0035197244 scopus 로고    scopus 로고
    • The Arabidopsis Somatic Embryogenesis Receptor Kinase 1 Gene Is Expressed in Developing Ovules and Embryos and Enhances Embryogenic Competence in Culture
    • Hecht V, Vielle-Calzada J-P, Hartog MV, Schmidt EDL, Boutilier K, et al. (2001) The Arabidopsis Somatic Embryogenesis Receptor Kinase 1 Gene Is Expressed in Developing Ovules and Embryos and Enhances Embryogenic Competence in Culture. Plant Physiol 127: 803-816.
    • (2001) Plant Physiol , vol.127 , pp. 803-816
    • Hecht, V.1    Vielle-Calzada, J.-P.2    Hartog, M.V.3    Schmidt, E.D.L.4    Boutilier, K.5
  • 17
    • 55549126848 scopus 로고    scopus 로고
    • Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways
    • Albrecht C, Russinova E, Kemmerling B, Kwaaitaal M, de Vries SC, (2008) Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and-independent signaling pathways. Plant Physiol 148: 611-619.
    • (2008) Plant Physiol , vol.148 , pp. 611-619
    • Albrecht, C.1    Russinova, E.2    Kemmerling, B.3    Kwaaitaal, M.4    de Vries, S.C.5
  • 18
    • 0037178782 scopus 로고    scopus 로고
    • BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling
    • Nam KH, Li J, (2002) BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling. Cell 110: 203-212.
    • (2002) Cell , vol.110 , pp. 203-212
    • Nam, K.H.1    Li, J.2
  • 19
    • 0037178776 scopus 로고    scopus 로고
    • BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling
    • Li J, Wen J, Lease KA, Doke JT, Tax FE, et al. (2002) BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Cell 110: 213-222.
    • (2002) Cell , vol.110 , pp. 213-222
    • Li, J.1    Wen, J.2    Lease, K.A.3    Doke, J.T.4    Tax, F.E.5
  • 20
    • 23944457745 scopus 로고    scopus 로고
    • Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase
    • Wang X, Goshe MB, Soderblom EJ, Phinney BS, Kuchar JA, et al. (2005) Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17: 1685-1703.
    • (2005) Plant Cell , vol.17 , pp. 1685-1703
    • Wang, X.1    Goshe, M.B.2    Soderblom, E.J.3    Phinney, B.S.4    Kuchar, J.A.5
  • 21
    • 48549096822 scopus 로고    scopus 로고
    • Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling
    • Wang X, Kota U, He K, Blackburn K, Li J, et al. (2008) Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling. Dev Cell 15: 220-235.
    • (2008) Dev Cell , vol.15 , pp. 220-235
    • Wang, X.1    Kota, U.2    He, K.3    Blackburn, K.4    Li, J.5
  • 22
    • 77953536732 scopus 로고    scopus 로고
    • BAK7 displays unequal genetic redundancy with BAK1 in brassinosteroid signaling and early senescence in arabidopsis
    • Jeong YJ, Shang Y, Kim BH, Kim SY, Song JH, et al. (2010) BAK7 displays unequal genetic redundancy with BAK1 in brassinosteroid signaling and early senescence in arabidopsis. Mol Cells 29: 259-266.
    • (2010) Mol Cells , vol.29 , pp. 259-266
    • Jeong, Y.J.1    Shang, Y.2    Kim, B.H.3    Kim, S.Y.4    Song, J.H.5
  • 23
    • 34250803478 scopus 로고    scopus 로고
    • The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in plant cell-death control
    • Kemmerling B, Schwedt A, Rodriguez P, Mazzotta S, Frank M, et al. (2007) The BRI1-associated kinase 1, BAK1, has a brassinolide-independent role in plant cell-death control. Curr Biol 17: 1116-1122.
    • (2007) Curr Biol , vol.17 , pp. 1116-1122
    • Kemmerling, B.1    Schwedt, A.2    Rodriguez, P.3    Mazzotta, S.4    Frank, M.5
  • 24
    • 34250872460 scopus 로고    scopus 로고
    • BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways
    • He K, Gou X, Yuan T, Lin H, Asami T, et al. (2007) BAK1 and BKK1 regulate brassinosteroid-dependent growth and brassinosteroid-independent cell-death pathways. Curr Biol 17: 1109-1115.
    • (2007) Curr Biol , vol.17 , pp. 1109-1115
    • He, K.1    Gou, X.2    Yuan, T.3    Lin, H.4    Asami, T.5
  • 25
    • 67651083654 scopus 로고    scopus 로고
    • Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis
    • Gao M, Wang X, Wang D, Xu F, Ding X, et al. (2009) Regulation of cell death and innate immunity by two receptor-like kinases in Arabidopsis. Cell Host Microbe 6: 34-44.
    • (2009) Cell Host Microbe , vol.6 , pp. 34-44
    • Gao, M.1    Wang, X.2    Wang, D.3    Xu, F.4    Ding, X.5
  • 26
    • 34547193514 scopus 로고    scopus 로고
    • The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants
    • Heese A, Hann DR, Gimenez-Ibanez S, Jones AM, He K, et al. (2007) The receptor-like kinase SERK3/BAK1 is a central regulator of innate immunity in plants. Proc Natl Acad Sci U S A 104: 12217-12222.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12217-12222
    • Heese, A.1    Hann, D.R.2    Gimenez-Ibanez, S.3    Jones, A.M.4    He, K.5
  • 27
    • 34547151023 scopus 로고    scopus 로고
    • A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence
    • Chinchilla D, Zipfel C, Robatzek S, Kemmerling B, Nurnberger T, et al. (2007) A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 448: 497-500.
    • (2007) Nature , vol.448 , pp. 497-500
    • Chinchilla, D.1    Zipfel, C.2    Robatzek, S.3    Kemmerling, B.4    Nurnberger, T.5
  • 28
    • 77951517299 scopus 로고    scopus 로고
    • Perception of the Arabidopsis danger signal peptide 1 involves the pattern recognition receptor AtPEPR1 and its close homologue AtPEPR2
    • Krol E, Mentzel T, Chinchilla D, Boller T, Felix G, et al. (2010) Perception of the Arabidopsis danger signal peptide 1 involves the pattern recognition receptor AtPEPR1 and its close homologue AtPEPR2. J Biol Chem 285: 13471-13479.
    • (2010) J Biol Chem , vol.285 , pp. 13471-13479
    • Krol, E.1    Mentzel, T.2    Chinchilla, D.3    Boller, T.4    Felix, G.5
  • 29
    • 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, He P, Li J, Heese A, Peck SC, et al. (2008) 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) Cell Host Microbe , vol.4 , pp. 17-27
    • Shan, L.1    He, P.2    Li, J.3    Heese, A.4    Peck, S.C.5
  • 30
    • 77951219239 scopus 로고    scopus 로고
    • Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1
    • Schulze B, Mentzel T, Jehle AK, Mueller K, Beeler S, et al. (2010) Rapid heteromerization and phosphorylation of ligand-activated plant transmembrane receptors and their associated kinase BAK1. J Biol Chem 285: 9444-9451.
    • (2010) J Biol Chem , vol.285 , pp. 9444-9451
    • Schulze, B.1    Mentzel, T.2    Jehle, A.K.3    Mueller, K.4    Beeler, S.5
  • 31
    • 40149083472 scopus 로고    scopus 로고
    • Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases
    • Xiang T, Zong N, Zou Y, Wu Y, Zhang J, et al. (2008) Pseudomonas syringae effector AvrPto blocks innate immunity by targeting receptor kinases. Curr Biol 18: 74-80.
    • (2008) Curr Biol , vol.18 , pp. 74-80
    • Xiang, T.1    Zong, N.2    Zou, Y.3    Wu, Y.4    Zhang, J.5
  • 32
    • 78650652060 scopus 로고    scopus 로고
    • BAK1 is not a target of the Pseudomonas syringae effector AvrPto
    • Xiang T, Zong N, Zhang J, Chen J, Chen M, et al. (2011) BAK1 is not a target of the Pseudomonas syringae effector AvrPto. Mol Plant Microbe Interact 24: 100-107.
    • (2011) Mol Plant Microbe Interact , vol.24 , pp. 100-107
    • Xiang, T.1    Zong, N.2    Zhang, J.3    Chen, J.4    Chen, M.5
  • 33
    • 12744273399 scopus 로고    scopus 로고
    • Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1
    • Kinoshita T, Cano-Delgado A, Seto H, Hiranuma S, Fujioka S, et al. (2005) Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1. Nature 433: 167-171.
    • (2005) Nature , vol.433 , pp. 167-171
    • Kinoshita, T.1    Cano-Delgado, A.2    Seto, H.3    Hiranuma, S.4    Fujioka, S.5
  • 34
    • 78049278937 scopus 로고    scopus 로고
    • Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression
    • Oh MH, Wang X, Wu X, Zhao Y, Clouse SD, et al. (2010) Autophosphorylation of Tyr-610 in the receptor kinase BAK1 plays a role in brassinosteroid signaling and basal defense gene expression. Proc Natl Acad Sci U S A 107: 17827-17832.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17827-17832
    • Oh, M.H.1    Wang, X.2    Wu, X.3    Zhao, Y.4    Clouse, S.D.5
  • 35
    • 33645776778 scopus 로고    scopus 로고
    • Plant and animal pathogen recognition receptors signal through non-RD kinases
    • doi:10.1371/journal.ppat.0020002
    • Dardick C, Ronald P, (2006) Plant and animal pathogen recognition receptors signal through non-RD kinases. PLoS Pathog 2: e2 doi:10.1371/journal.ppat.0020002.
    • (2006) PLoS Pathog , vol.2
    • Dardick, C.1    Ronald, P.2
  • 36
    • 70350755586 scopus 로고    scopus 로고
    • Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity
    • Nekrasov V, Li J, Batoux M, Roux M, Chu ZH, et al. (2009) Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity. Embo J 28: 3428-3438.
    • (2009) Embo J , vol.28 , pp. 3428-3438
    • Nekrasov, V.1    Li, J.2    Batoux, M.3    Roux, M.4    Chu, Z.H.5
  • 37
    • 77949773101 scopus 로고    scopus 로고
    • Differential innate immune signalling via Ca(2+) sensor protein kinases
    • Boudsocq M, Willmann MR, McCormack M, Lee H, Shan L, et al. (2010) Differential innate immune signalling via Ca(2+) sensor protein kinases. Nature 464: 418-422.
    • (2010) Nature , vol.464 , pp. 418-422
    • Boudsocq, M.1    Willmann, M.R.2    McCormack, M.3    Lee, H.4    Shan, L.5
  • 39
    • 33646134105 scopus 로고    scopus 로고
    • Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in Arabidopsis innate immunity
    • He P, Shan L, Lin NC, Martin GB, Kemmerling B, et al. (2006) Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in Arabidopsis innate immunity. Cell 125: 563-575.
    • (2006) Cell , vol.125 , pp. 563-575
    • He, P.1    Shan, L.2    Lin, N.C.3    Martin, G.B.4    Kemmerling, B.5
  • 40
    • 33748129962 scopus 로고    scopus 로고
    • Plant stomata function in innate immunity against bacterial invasion
    • Melotto M, Underwood W, Koczan J, Nomura K, He SY, (2006) Plant stomata function in innate immunity against bacterial invasion. Cell 126: 969-980.
    • (2006) Cell , vol.126 , pp. 969-980
    • Melotto, M.1    Underwood, W.2    Koczan, J.3    Nomura, K.4    He, S.Y.5
  • 41
    • 0020046406 scopus 로고
    • Synthesis of brassinosteroids and relationship of structure to plant growth-promoting effects
    • Thompson MJ, Meudt WJ, Mandava NB, Dutky SR, Lusby WR, et al. (1982) Synthesis of brassinosteroids and relationship of structure to plant growth-promoting effects. Steroids 39: 89-105.
    • (1982) Steroids , vol.39 , pp. 89-105
    • Thompson, M.J.1    Meudt, W.J.2    Mandava, N.B.3    Dutky, S.R.4    Lusby, W.R.5
  • 42
    • 0034788890 scopus 로고    scopus 로고
    • Brassinazole, an inhibitor of brassinosteroid biosynthesis, inhibits development of secondary xylem in cress plants (Lepidium sativum)
    • Nagata N, Asami T, Yoshida S, (2001) Brassinazole, an inhibitor of brassinosteroid biosynthesis, inhibits development of secondary xylem in cress plants (Lepidium sativum). Plant Cell Physiol 42: 1006-1011.
    • (2001) Plant Cell Physiol , vol.42 , pp. 1006-1011
    • Nagata, N.1    Asami, T.2    Yoshida, S.3
  • 44
    • 1942501811 scopus 로고    scopus 로고
    • Comprehensive comparison of auxin-regulated and brassinosteroid-regulated genes in Arabidopsis
    • Goda H, Sawa S, Asami T, Fujioka S, Shimada Y, et al. (2004) Comprehensive comparison of auxin-regulated and brassinosteroid-regulated genes in Arabidopsis. Plant Physiol 134: 1555-1573.
    • (2004) Plant Physiol , vol.134 , pp. 1555-1573
    • Goda, H.1    Sawa, S.2    Asami, T.3    Fujioka, S.4    Shimada, Y.5
  • 45
    • 18344371419 scopus 로고    scopus 로고
    • Nuclear-localized BZR1 mediates brassinosteroid-induced growth and feedback suppression of brassinosteroid biosynthesis
    • Wang ZY, Nakano T, Gendron J, He J, Chen M, et al. (2002) Nuclear-localized BZR1 mediates brassinosteroid-induced growth and feedback suppression of brassinosteroid biosynthesis. Dev Cell 2: 505-513.
    • (2002) Dev Cell , vol.2 , pp. 505-513
    • Wang, Z.Y.1    Nakano, T.2    Gendron, J.3    He, J.4    Chen, M.5
  • 46
    • 77952507231 scopus 로고    scopus 로고
    • Brassinosteroid signal transduction from receptor kinases to transcription factors
    • Kim TW, Wang ZY, (2010) Brassinosteroid signal transduction from receptor kinases to transcription factors. Annu Rev Plant Biol 61: 681-704.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 681-704
    • Kim, T.W.1    Wang, Z.Y.2
  • 47
    • 41849105780 scopus 로고    scopus 로고
    • Is kinase activity essential for biological functions of BRI1?
    • Xu W, Huang J, Li B, Li J, Wang Y, (2008) Is kinase activity essential for biological functions of BRI1? Cell Res 18: 472-478.
    • (2008) Cell Res , vol.18 , pp. 472-478
    • Xu, W.1    Huang, J.2    Li, B.3    Li, J.4    Wang, Y.5
  • 48
    • 37649023555 scopus 로고    scopus 로고
    • CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
    • Miya A, Albert P, Shinya T, Desaki Y, Ichimura K, et al. (2007) CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc Natl Acad Sci U S A 104: 19613-19618.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19613-19618
    • Miya, A.1    Albert, P.2    Shinya, T.3    Desaki, Y.4    Ichimura, K.5
  • 49
    • 45149090440 scopus 로고    scopus 로고
    • A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis
    • Wan J, Zhang XC, Neece D, Ramonell KM, Clough S, et al. (2008) A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis. Plant Cell 20: 471-481.
    • (2008) Plant Cell , vol.20 , pp. 471-481
    • Wan, J.1    Zhang, X.C.2    Neece, D.3    Ramonell, K.M.4    Clough, S.5
  • 50
    • 76249083550 scopus 로고    scopus 로고
    • A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity
    • Lu D, Wu S, Gao X, Zhang Y, Shan L, et al. (2010) A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity. Proc Natl Acad Sci U S A 107: 496-501.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 496-501
    • Lu, D.1    Wu, S.2    Gao, X.3    Zhang, Y.4    Shan, L.5
  • 51
    • 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, (2001) 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) Plant Cell , vol.13 , pp. 1155-1163
    • Gomez-Gomez, L.1    Bauer, Z.2    Boller, T.3
  • 52
    • 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, Li W, Xiang T, Liu Z, Laluk K, et al. (2010) 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) Cell Host Microbe , vol.7 , pp. 290-301
    • Zhang, J.1    Li, W.2    Xiang, T.3    Liu, Z.4    Laluk, K.5
  • 53
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J, (2010) Cell signaling by receptor tyrosine kinases. Cell 141: 1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 55
    • 77952396347 scopus 로고    scopus 로고
    • An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity
    • Chen X, Chern M, Canlas PE, Ruan D, Jiang C, et al. (2010) An ATPase promotes autophosphorylation of the pattern recognition receptor XA21 and inhibits XA21-mediated immunity. Proc Natl Acad Sci U S A 107: 8029-8034.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 8029-8034
    • Chen, X.1    Chern, M.2    Canlas, P.E.3    Ruan, D.4    Jiang, C.5
  • 56
    • 70349452803 scopus 로고    scopus 로고
    • Receptor-like protein kinases, BAK1 and BKK1, regulate a light-dependent cell-death control pathway
    • He K, Gou X, Powell RA, Yang H, Yuan T, et al. (2008) Receptor-like protein kinases, BAK1 and BKK1, regulate a light-dependent cell-death control pathway. Plant Signal Behav 3: 813-815.
    • (2008) Plant Signal Behav , vol.3 , pp. 813-815
    • He, K.1    Gou, X.2    Powell, R.A.3    Yang, H.4    Yuan, T.5
  • 57
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: towards an integrated view of plant-pathogen interactions
    • Dodds PN, Rathjen JP, (2010) Plant immunity: towards an integrated view of plant-pathogen interactions. Nat Rev Genet 11: 539-548.
    • (2010) Nat Rev Genet , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 58
    • 0030469482 scopus 로고    scopus 로고
    • Giant protein kinases: domain interactions and structural basis of autoregulation
    • Kobe B, Heierhorst J, Feil SC, Parker MW, Benian GM, et al. (1996) Giant protein kinases: domain interactions and structural basis of autoregulation. Embo J 15: 6810-6821.
    • (1996) Embo J , vol.15 , pp. 6810-6821
    • Kobe, B.1    Heierhorst, J.2    Feil, S.C.3    Parker, M.W.4    Benian, G.M.5
  • 59
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans O, van der Ven PF, Wilm M, Mues A, Young P, et al. (1998) Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395: 863-869.
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    van der Ven, P.F.2    Wilm, M.3    Mues, A.4    Young, P.5
  • 60
    • 0035155003 scopus 로고    scopus 로고
    • The structure of Sky1p reveals a novel mechanism for constitutive activity
    • Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, et al. (2001) The structure of Sky1p reveals a novel mechanism for constitutive activity. Nat Struct Biol 8: 176-183.
    • (2001) Nat Struct Biol , vol.8 , pp. 176-183
    • Nolen, B.1    Yun, C.Y.2    Wong, C.F.3    McCammon, J.A.4    Fu, X.D.5
  • 61
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan E, Tschopp J, (2005) The RIP kinases: crucial integrators of cellular stress. Trends Biochem Sci 30: 151-159.
    • (2005) Trends Biochem Sci , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 62
    • 0028341134 scopus 로고
    • The glycine-rich sequence of protein kinases: a multifunctional element
    • Bossemeyer D, (1994) The glycine-rich sequence of protein kinases: a multifunctional element. Trends Biochem Sci 19: 201-205.
    • (1994) Trends Biochem Sci , vol.19 , pp. 201-205
    • Bossemeyer, D.1
  • 63
    • 0033061031 scopus 로고    scopus 로고
    • Catalytic subunit of cyclic AMP-dependent protein kinase: structure and dynamics of the active site cleft
    • Taylor SS, Radzio-Andzelm E, Madhusudan, Cheng X, Ten Eyck L, et al. (1999) Catalytic subunit of cyclic AMP-dependent protein kinase: structure and dynamics of the active site cleft. Pharmacol Ther 82: 133-141.
    • (1999) Pharmacol Ther , vol.82 , pp. 133-141
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Madhusudan3    Cheng, X.4    Ten Eyck, L.5
  • 64
    • 33644872221 scopus 로고    scopus 로고
    • The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase
    • Xu WH, Wang YS, Liu GZ, Chen X, Tinjuangjun P, et al. (2006) The autophosphorylated Ser686, Thr688, and Ser689 residues in the intracellular juxtamembrane domain of XA21 are implicated in stability control of rice receptor-like kinase. Plant J 45: 740-751.
    • (2006) Plant J , vol.45 , pp. 740-751
    • Xu, W.H.1    Wang, Y.S.2    Liu, G.Z.3    Chen, X.4    Tinjuangjun, P.5
  • 65
    • 77951226283 scopus 로고    scopus 로고
    • A conserved threonine residue in the juxtamembrane domain of the XA21 pattern recognition receptor is critical for kinase autophosphorylation and XA21-mediated immunity
    • Chen X, Chern M, Canlas PE, Jiang C, Ruan D, et al. (2010) A conserved threonine residue in the juxtamembrane domain of the XA21 pattern recognition receptor is critical for kinase autophosphorylation and XA21-mediated immunity. J Biol Chem.
    • (2010) J Biol Chem
    • Chen, X.1    Chern, M.2    Canlas, P.E.3    Jiang, C.4    Ruan, D.5
  • 66
    • 0037186599 scopus 로고    scopus 로고
    • MAP kinase signalling cascade in Arabidopsis innate immunity
    • Asai T, Tena G, Plotnikova J, Willmann MR, Chiu WL, et al. (2002) MAP kinase signalling cascade in Arabidopsis innate immunity. Nature 415: 977-983.
    • (2002) Nature , vol.415 , pp. 977-983
    • Asai, T.1    Tena, G.2    Plotnikova, J.3    Willmann, M.R.4    Chiu, W.L.5
  • 67
    • 33644780918 scopus 로고    scopus 로고
    • Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis
    • Robatzek S, Chinchilla D, Boller T, (2006) Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. Genes Dev 20: 537-542.
    • (2006) Genes Dev , vol.20 , pp. 537-542
    • Robatzek, S.1    Chinchilla, D.2    Boller, T.3
  • 68
    • 0036890406 scopus 로고    scopus 로고
    • Web-based primer design for single nucleotide polymorphism analysis
    • Neff MM, Turk E, Kalishman M, (2002) Web-based primer design for single nucleotide polymorphism analysis. Trends Genet 18: 613-615.
    • (2002) Trends Genet , vol.18 , pp. 613-615
    • Neff, M.M.1    Turk, E.2    Kalishman, M.3
  • 69
    • 34547677722 scopus 로고    scopus 로고
    • Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation
    • Nakagawa T, Kurose T, Hino T, Tanaka K, Kawamukai M, et al. (2007) Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. J Biosci Bioeng 104: 34-41.
    • (2007) J Biosci Bioeng , vol.104 , pp. 34-41
    • Nakagawa, T.1    Kurose, T.2    Hino, T.3    Tanaka, K.4    Kawamukai, M.5
  • 70
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF, (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 71
    • 60349099902 scopus 로고    scopus 로고
    • Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases
    • Karlova R, Boeren S, van Dongen W, Kwaaitaal M, Aker J, et al. (2009) Identification of in vitro phosphorylation sites in the Arabidopsis thaliana somatic embryogenesis receptor-like kinases. Proteomics 9: 368-379.
    • (2009) Proteomics , vol.9 , pp. 368-379
    • Karlova, R.1    Boeren, S.2    van Dongen, W.3    Kwaaitaal, M.4    Aker, J.5
  • 72
    • 34247846396 scopus 로고    scopus 로고
    • A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
    • Berrow NS, Alderton D, Sainsbury S, Nettleship J, Assenberg R, et al. (2007) A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res 35: e45.
    • (2007) Nucleic Acids Res , vol.35
    • Berrow, N.S.1    Alderton, D.2    Sainsbury, S.3    Nettleship, J.4    Assenberg, R.5
  • 74
    • 33644872218 scopus 로고    scopus 로고
    • Gateway-compatible vectors for plant functional genomics and proteomics
    • Earley KW, Haag JR, Pontes O, Opper K, Juehne T, et al. (2006) Gateway-compatible vectors for plant functional genomics and proteomics. Plant J 45: 616-629.
    • (2006) Plant J , vol.45 , pp. 616-629
    • Earley, K.W.1    Haag, J.R.2    Pontes, O.3    Opper, K.4    Juehne, T.5
  • 75
    • 61449086250 scopus 로고    scopus 로고
    • AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants
    • Gimenez-Ibanez S, Hann DR, Ntoukakis V, Petutschnig E, Lipka V, et al. (2009) AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants. Curr Biol 19: 423-429.
    • (2009) Curr Biol , vol.19 , pp. 423-429
    • Gimenez-Ibanez, S.1    Hann, D.R.2    Ntoukakis, V.3    Petutschnig, E.4    Lipka, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.