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Volumn 108, Issue 52, 2011, Pages 21259-21264

Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases

Author keywords

[No Author keywords available]

Indexed keywords

ABSCISIC ACID; CYCLIN DEPENDENT KINASE; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; PHOSPHOTRANSFERASE; SNF1 RELATED KINASE 2.3; SNF1 RELATED KINASE 2.6; UNCLASSIFIED DRUG;

EID: 84862950886     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1118651109     Document Type: Article
Times cited : (141)

References (50)
  • 1
    • 39549088882 scopus 로고    scopus 로고
    • Abscisic Acid and abiotic stress signaling
    • Tuteja N (2007) Abscisic Acid and abiotic stress signaling. Plant Signal Behav 2:135-138.
    • (2007) Plant Signal Behav , vol.2 , pp. 135-138
    • Tuteja, N.1
  • 2
    • 71449104756 scopus 로고    scopus 로고
    • In vitro reconstitution of an abscisic acid signalling pathway
    • Fujii H, et al. (2009) In vitro reconstitution of an abscisic acid signalling pathway. Nature 462:660-664.
    • (2009) Nature , vol.462 , pp. 660-664
    • Fujii, H.1
  • 3
    • 70350468918 scopus 로고    scopus 로고
    • Type 2C protein phosphatases directly regulate abscisic acid-activated protein kinases in Arabidopsis
    • Umezawa T, et al. (2009) Type 2C protein phosphatases directly regulate abscisic acid-activated protein kinases in Arabidopsis. Proc Natl Acad Sci USA 106:17588-17593.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17588-17593
    • Umezawa, T.1
  • 4
    • 66249083481 scopus 로고    scopus 로고
    • Arabidopsis mutant deficient in 3 abscisic acid-activated protein kinases reveals critical roles in growth, reproduction, and stress
    • Fujii H, Zhu JK (2009) Arabidopsis mutant deficient in 3 abscisic acid-activated protein kinases reveals critical roles in growth, reproduction, and stress. Proc Natl Acad Sci USA 106:8380-8385.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8380-8385
    • Fujii, H.1    Zhu, J.K.2
  • 6
    • 33847208920 scopus 로고    scopus 로고
    • Different phosphorylation mechanisms are involved in the activation of sucrose non-fermenting 1 related protein kinases 2 by osmotic stresses and abscisic acid
    • Boudsocq M, Droillard MJ, Barbier-Brygoo H, Laurière C (2007) Different phosphorylation mechanisms are involved in the activation of sucrose non-fermenting 1 related protein kinases 2 by osmotic stresses and abscisic acid. Plant Mol Biol 63:491-503.
    • (2007) Plant Mol Biol , vol.63 , pp. 491-503
    • Boudsocq, M.1    Droillard, M.J.2    Barbier-Brygoo, H.3    Laurière, C.4
  • 8
    • 77955885246 scopus 로고    scopus 로고
    • Early abscisic acid signal transduction mechanisms: Newly discovered components and newly emerging questions
    • Hubbard KE, Nishimura N, Hitomi K, Getzoff ED, Schroeder JI (2010) Early abscisic acid signal transduction mechanisms: Newly discovered components and newly emerging questions. Genes Dev 24:1695-1708.
    • (2010) Genes Dev , vol.24 , pp. 1695-1708
    • Hubbard, K.E.1    Nishimura, N.2    Hitomi, K.3    Getzoff, E.D.4    Schroeder, J.I.5
  • 9
    • 71449087943 scopus 로고    scopus 로고
    • Structural insights into the mechanism of abscisic acid signaling by PYL proteins
    • Yin P, et al. (2009) Structural insights into the mechanism of abscisic acid signaling by PYL proteins. Nat Struct Mol Biol 16:1230-1236.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1230-1236
    • Yin, P.1
  • 10
    • 66249133969 scopus 로고    scopus 로고
    • Regulators of PP2C phosphatase activity function as abscisic acid sensors
    • Ma Y, et al. (2009) Regulators of PP2C phosphatase activity function as abscisic acid sensors. Science 324:1064-1068.
    • (2009) Science , vol.324 , pp. 1064-1068
    • Ma, Y.1
  • 11
    • 66249110335 scopus 로고    scopus 로고
    • Abscisic acid inhibits type 2C protein phosphatases via the PYR/ PYL family of START proteins
    • Park SY, et al. (2009) Abscisic acid inhibits type 2C protein phosphatases via the PYR/ PYL family of START proteins. Science 324:1068-1071.
    • (2009) Science , vol.324 , pp. 1068-1071
    • Park, S.Y.1
  • 12
    • 72049093208 scopus 로고    scopus 로고
    • Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis
    • Vlad F, et al. (2009) Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis. Plant Cell 21:3170-3184.
    • (2009) Plant Cell , vol.21 , pp. 3170-3184
    • Vlad, F.1
  • 13
    • 71449125748 scopus 로고    scopus 로고
    • A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors
    • Melcher K, et al. (2009) A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors. Nature 462:602-608.
    • (2009) Nature , vol.462 , pp. 602-608
    • Melcher, K.1
  • 14
    • 71449110803 scopus 로고    scopus 로고
    • Structural basis of abscisic acid signalling
    • Miyazono K, et al. (2009) Structural basis of abscisic acid signalling. Nature 462: 609-614.
    • (2009) Nature , vol.462 , pp. 609-614
    • Miyazono, K.1
  • 15
    • 71449098436 scopus 로고    scopus 로고
    • Structural mechanism of abscisic acid binding and signaling by dimeric PYR1
    • Nishimura N, et al. (2009) Structural mechanism of abscisic acid binding and signaling by dimeric PYR1. Science 326:1373-1379.
    • (2009) Science , vol.326 , pp. 1373-1379
    • Nishimura, N.1
  • 16
    • 71449125712 scopus 로고    scopus 로고
    • The abscisic acid receptor PYR1 in complex with abscisic acid
    • Santiago J, et al. (2009) The abscisic acid receptor PYR1 in complex with abscisic acid. Nature 462:665-668.
    • (2009) Nature , vol.462 , pp. 665-668
    • Santiago, J.1
  • 17
    • 77956549302 scopus 로고    scopus 로고
    • Functional mechanism of the abscisic acid agonist pyrabactin
    • Hao Q, et al. (2010) Functional mechanism of the abscisic acid agonist pyrabactin. J Biol Chem 285:28946-28952.
    • (2010) J Biol Chem , vol.285 , pp. 28946-28952
    • Hao, Q.1
  • 18
    • 77956345169 scopus 로고    scopus 로고
    • Identification and mechanism of ABA receptor antagonism
    • Melcher K, et al. (2010) Identification and mechanism of ABA receptor antagonism. Nat Struct Mol Biol 17:1102-1108.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1102-1108
    • Melcher, K.1
  • 19
    • 77956341748 scopus 로고    scopus 로고
    • Structural basis for selective activation of ABA receptors
    • Peterson FC, et al. (2010) Structural basis for selective activation of ABA receptors. Nat Struct Mol Biol 17:1109-1113.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 1109-1113
    • Peterson, F.C.1
  • 21
    • 0036801466 scopus 로고    scopus 로고
    • The abscisic acid-responsive kinase PKABA1 interacts with a seed-specific abscisic acid response element-binding factor, TaABF, and phosphorylates TaABF peptide sequences
    • DOI 10.1104/pp.001354
    • Johnson RR, Wagner RL, Verhey SD, Walker-Simmons MK (2002) The abscisic acidresponsive kinase PKABA1 interacts with a seed-specific abscisic acid response element-binding factor, TaABF, and phosphorylates TaABF peptide sequences. Plant Physiol 130:837-846. (Pubitemid 35224786)
    • (2002) Plant Physiology , vol.130 , Issue.2 , pp. 837-846
    • Johnson, R.R.1    Wagner, R.L.2    Verhey, S.D.3    Walker-Simmons, M.K.4
  • 22
    • 84855477482 scopus 로고    scopus 로고
    • Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases
    • 10.1126/science.1215106
    • Soon F.-F., et al. (2011) Molecular mimicry regulates ABA signaling by SnRK2 kinases and PP2C phosphatases. Science, 10.1126/science.1215106.
    • (2011) Science
    • Soon, F.-F.1
  • 23
    • 62349091524 scopus 로고    scopus 로고
    • Protein kinase activation loop autophosphorylation in cis: Overcoming a Catch-22 situation
    • Lochhead PA (2009) Protein kinase activation loop autophosphorylation in cis: Overcoming a Catch-22 situation. Sci Signal 2:pe4.
    • (2009) Sci Signal , vol.2
    • Lochhead, P.A.1
  • 24
    • 78951473056 scopus 로고    scopus 로고
    • Mechanistic studies of the autoactivation of PAK2: A two-step model of cis initiation followed by trans amplification
    • Wang J, Wu JW, Wang ZX (2011) Mechanistic studies of the autoactivation of PAK2: A two-step model of cis initiation followed by trans amplification. J Biol Chem 286:2689-2695.
    • (2011) J Biol Chem , vol.286 , pp. 2689-2695
    • Wang, J.1    Wu, J.W.2    Wang, Z.X.3
  • 25
    • 76349093842 scopus 로고    scopus 로고
    • A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation
    • Littler DR, et al. (2010) A conserved mechanism of autoinhibition for the AMPK kinase domain: ATP-binding site and catalytic loop refolding as a means of regulation. Acta Crystallogr Sect F Struct Biol Cryst Commun 66:143-151.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 143-151
    • Littler, D.R.1
  • 26
    • 36049032359 scopus 로고    scopus 로고
    • A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions
    • Chalmers MJ, Busby SA, Pascal BD, Southern MR, Griffin PR (2007) A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions. J Biomol Tech 18:194-204.
    • (2007) J Biomol Tech , vol.18 , pp. 194-204
    • Chalmers, M.J.1    Busby, S.A.2    Pascal, B.D.3    Southern, M.R.4    Griffin, P.R.5
  • 27
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda ZS (2004) Rational protein crystallization by mutational surface engineering. Structure 12:529-535.
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 29
    • 67649484365 scopus 로고    scopus 로고
    • Structural insight into the autoinhibition mechanism of AMP activated protein kinase
    • Chen L, et al. (2009) Structural insight into the autoinhibition mechanism of AMP activated protein kinase. Nature 459:1146-1149.
    • (2009) Nature , vol.459 , pp. 1146-1149
    • Chen, L.1
  • 30
    • 33644833886 scopus 로고    scopus 로고
    • Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family
    • DOI 10.1016/j.str.2005.12.008, PII S0969212606000682
    • Nayak V, et al. (2006) Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family. Structure 14:477-485. (Pubitemid 43363481)
    • (2006) Structure , vol.14 , Issue.3 , pp. 477-485
    • Nayak, V.1    Zhao, K.2    Wyce, A.3    Schwartz, M.F.4    Lo, W.-S.5    Berger, S.L.6    Marmorstein, R.7
  • 32
    • 77950215269 scopus 로고    scopus 로고
    • Proteus in the world of proteins: Conformational changes in protein kinases
    • Rabiller M, et al. (2010) Proteus in the world of proteins: Conformational changes in protein kinases. Arch Pharm (Weinheim) 343:193-206.
    • (2010) Arch Pharm (Weinheim) , vol.343 , pp. 193-206
    • Rabiller, M.1
  • 33
    • 0033574614 scopus 로고    scopus 로고
    • Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors
    • Pavletich NP (1999) Mechanisms of cyclin-dependent kinase regulation: Structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors. J Mol Biol 287:821-828.
    • (1999) J Mol Biol , vol.287 , pp. 821-828
    • Pavletich, N.P.1
  • 34
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • Nolen B, Taylor S, Ghosh G (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 15:661-675. (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 35
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey PD, et al. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376:313-320.
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1
  • 36
    • 77953510471 scopus 로고    scopus 로고
    • Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases
    • Marx A, Nugoor C, Panneerselvam S, Mandelkow E (2010) Structure and function of polarity-inducing kinase family MARK/Par-1 within the branch of AMPK/Snf1-related kinases. FASEB J 24:1637-1648.
    • (2010) FASEB J , vol.24 , pp. 1637-1648
    • Marx, A.1    Nugoor, C.2    Panneerselvam, S.3    Mandelkow, E.4
  • 38
    • 33745002702 scopus 로고    scopus 로고
    • An Allosteric Mechanism for Activation of the Kinase Domain of Epidermal Growth Factor Receptor
    • DOI 10.1016/j.cell.2006.05.013, PII S0092867406005848
    • Zhang X, Gureasko J, Shen K, Cole PA, Kuriyan J (2006) An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125:1137-1149. (Pubitemid 43866200)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 39
    • 0033555270 scopus 로고    scopus 로고
    • Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine
    • DOI 10.1006/jmbi.1998.2369
    • Lamers MB, Antson AA, Hubbard RE, Scott RK, Williams DH (1999) Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine. J Mol Biol 285:713-725. (Pubitemid 29041803)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.2 , pp. 713-725
    • Lamers, M.B.A.C.1    Antson, A.A.2    Hubbard, R.E.3    Scott, R.K.4    Williams, D.H.5
  • 40
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • DOI 10.1016/S1097-2765(03)00392-7
    • Bayliss R, Sardon T, Vernos I, Conti E (2003) Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol Cell 12:851-862. (Pubitemid 37352779)
    • (2003) Molecular Cell , vol.12 , Issue.4 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 41
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:275-282. (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 43
    • 81055157640 scopus 로고    scopus 로고
    • The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress
    • Yunta C, Martínez-Ripoll M, Zhu JK, Albert A (2011) The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress. J Mol Biol 414:135-144.
    • (2011) J Mol Biol , vol.414 , pp. 135-144
    • Yunta, C.1    Martínez-Ripoll, M.2    Zhu, J.K.3    Albert, A.4
  • 49
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54:905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.T.1


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