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Volumn 414, Issue 1, 2011, Pages 135-144

The structure of arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress

Author keywords

crystallography; kinase regulation; plant abiotic stress; protein structure; signaling

Indexed keywords

ABSCISIC ACID; ARABIDOPSIS PROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2C; PROTEIN OPEN STOMATA 1; SNF1 RELATED PROTEIN KINASE 2; UNCLASSIFIED DRUG;

EID: 81055157640     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.09.041     Document Type: Article
Times cited : (35)

References (60)
  • 1
    • 79952146183 scopus 로고    scopus 로고
    • Arabidopsis decuple mutant reveals the importance of SnRK2 kinases in osmotic stress responses in vivo
    • Fujii H., Verslues P.E., and Zhu J.K. Arabidopsis decuple mutant reveals the importance of SnRK2 kinases in osmotic stress responses in vivo Proc. Natl Acad. Sci. USA 108 2011 1717 1722
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1717-1722
    • Fujii, H.1    Verslues, P.E.2    Zhu, J.K.3
  • 2
    • 34248185047 scopus 로고    scopus 로고
    • Regulatory metabolic networks in drought stress responses
    • DOI 10.1016/j.pbi.2007.04.014, PII S1369526607000490, Physiology and Metabolism Edited by Clint Chapple and Malcolm M Campbell
    • Seki M., Umezawa T., Urano K., and Shinozaki K. Regulatory metabolic networks in drought stress responses Curr. Opin. Plant Biol. 10 2007 296 302 (Pubitemid 46710486)
    • (2007) Current Opinion in Plant Biology , vol.10 , Issue.3 , pp. 296-302
    • Seki, M.1    Umezawa, T.2    Urano, K.3    Shinozaki, K.4
  • 5
    • 0141502038 scopus 로고    scopus 로고
    • Regulation of ion homeostasis under salt stress
    • Zhu J.K. Regulation of ion homeostasis under salt stress Curr. Opin. Plant Biol. 6 2003 441 445
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 441-445
    • Zhu, J.K.1
  • 6
    • 0035861897 scopus 로고    scopus 로고
    • Guard cell signaling
    • DOI 10.1016/S0092-8674(01)00606-7
    • Hetherington A.M. Guard cell signaling Cell 107 2001 711 714 (Pubitemid 34033664)
    • (2001) Cell , vol.107 , Issue.6 , pp. 711-714
    • Hetherington, A.M.1
  • 7
    • 0035868751 scopus 로고    scopus 로고
    • Guard cell abscisic acid signalling and engineering drought hardiness in plants
    • DOI 10.1038/35066500
    • Schroeder J.I., Kwak J.M., and Allen G.J. Guard cell abscisic acid signalling and engineering of drought hardiness in plants Nature 410 2001 327 330 (Pubitemid 32246041)
    • (2001) Nature , vol.410 , Issue.6826 , pp. 327-330
    • Schroeder, J.I.1    Kwak, J.M.2    Allen, G.J.3
  • 9
    • 33746777825 scopus 로고    scopus 로고
    • Different Plant Hormones Regulate Similar Processes through Largely Nonoverlapping Transcriptional Responses
    • DOI 10.1016/j.cell.2006.05.050, PII S0092867406009111
    • Nemhauser J.L., Hong F., and Chory J. Different plant hormones regulate similar processes through largely nonoverlapping transcriptional responses Cell 126 2006 467 475 (Pubitemid 44163606)
    • (2006) Cell , vol.126 , Issue.3 , pp. 467-475
    • Nemhauser, J.L.1    Hong, F.2    Chory, J.3
  • 10
    • 64249149813 scopus 로고    scopus 로고
    • Snf1-related protein kinases (SnRKs) act within an intricate network that links metabolic and stress signalling in plants
    • Halford N.G., and Hey S.J. Snf1-related protein kinases (SnRKs) act within an intricate network that links metabolic and stress signalling in plants Biochem. J. 419 2009 247 259
    • (2009) Biochem. J. , vol.419 , pp. 247-259
    • Halford, N.G.1    Hey, S.J.2
  • 11
  • 12
    • 66249110335 scopus 로고    scopus 로고
    • Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins
    • Park S.Y., Fung P., Nishimura N., Jensen D.R., Fujii H., and Zhao Y. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins Science 324 2009 1068 1071
    • (2009) Science , vol.324 , pp. 1068-1071
    • Park, S.Y.1    Fung, P.2    Nishimura, N.3    Jensen, D.R.4    Fujii, H.5    Zhao, Y.6
  • 14
    • 72049093208 scopus 로고    scopus 로고
    • Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis
    • Vlad F., Rubio S., Rodrigues A., Sirichandra C., Belin C., and Robert N. Protein phosphatases 2C regulate the activation of the Snf1-related kinase OST1 by abscisic acid in Arabidopsis Plant Cell. 21 2009 3170 3184
    • (2009) Plant Cell. , vol.21 , pp. 3170-3184
    • Vlad, F.1    Rubio, S.2    Rodrigues, A.3    Sirichandra, C.4    Belin, C.5    Robert, N.6
  • 15
    • 75849136096 scopus 로고    scopus 로고
    • A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signalling in plant guard cells
    • Lee S.C., Lan W., Buchanan B.B., and Luan S. A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signalling in plant guard cells Proc. Natl Acad. Sci. USA 106 2009 21419 21424
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 21419-21424
    • Lee, S.C.1    Lan, W.2    Buchanan, B.B.3    Luan, S.4
  • 16
    • 71449098436 scopus 로고    scopus 로고
    • Structural mechanism of abscisic acid binding and signalling by dimeric PYR1
    • Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C., and Cutler S.R. Structural mechanism of abscisic acid binding and signalling by dimeric PYR1 Science 326 2009 1373 1379
    • (2009) Science , vol.326 , pp. 1373-1379
    • Nishimura, N.1    Hitomi, K.2    Arvai, A.S.3    Rambo, R.P.4    Hitomi, C.5    Cutler, S.R.6
  • 19
    • 33646187177 scopus 로고    scopus 로고
    • The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis
    • DOI 10.1074/jbc.M509820200
    • Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F., and Shinozaki K. The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis J. Biol. Chem. 281 2006 5310 5318 (Pubitemid 43847795)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 5310-5318
    • Yoshida, R.1    Umezawa, T.2    Mizoguchi, T.3    Takahashi, S.4    Takahashi, F.5    Shinozaki, K.6
  • 21
    • 0036910331 scopus 로고    scopus 로고
    • Arabidopsis OST1 protein kinase mediates the regulation of stomatal aperture by abscisic acid and acts upstream of reactive oxygen species production
    • DOI 10.1105/tpc.007906
    • Mustilli A.C., Merlot S., Vavasseur A., Fenzi F., and Giraudat J. Arabidopsis OST1 protein kinase mediates the regulation of stomatal aperture by abscisic acid and acts upstream of reactive oxygen species production Plant Cell. 14 2002 3089 3099 (Pubitemid 36029134)
    • (2002) Plant Cell , vol.14 , Issue.12 , pp. 3089-3099
    • Mustilli, A.-C.1    Merlot, S.2    Vavasseur, A.3    Fenzi, F.4    Giraudat, J.5
  • 22
    • 73149112823 scopus 로고    scopus 로고
    • Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2/OST1/SnRK2.6 protein kinase
    • Sato A., Sato Y., Fukao Y., Fujiwara M., Umezawa T., and Shinozaki K. Threonine at position 306 of the KAT1 potassium channel is essential for channel activity and is a target site for ABA-activated SnRK2/OST1/SnRK2.6 protein kinase Biochem. J. 424 2009 439 448
    • (2009) Biochem. J. , vol.424 , pp. 439-448
    • Sato, A.1    Sato, Y.2    Fukao, Y.3    Fujiwara, M.4    Umezawa, T.5    Shinozaki, K.6
  • 23
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L., and Rosenström P. Dali server: conservation mapping in 3D Nucleic Acids Res. 38 2010 W545 W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 24
    • 67649484365 scopus 로고    scopus 로고
    • Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
    • Chen L., Jiao Z.H., Zheng L.S., Zhang Y.Y., Xie S.T., Wang Z.X., and Wu J.W. Structural insight into the autoinhibition mechanism of AMP-activated protein kinase Nature 459 2009 1146 1149
    • (2009) Nature , vol.459 , pp. 1146-1149
    • Chen, L.1    Jiao, Z.H.2    Zheng, L.S.3    Zhang, Y.Y.4    Xie, S.T.5    Wang, Z.X.6    Wu, J.W.7
  • 25
    • 0032847133 scopus 로고    scopus 로고
    • 600 ps molecular dynamics reveals stable substructures and flexible hinge points in cAMP dependent protein kinase
    • DOI 10.1002/(SICI)1097-0282(19991015)50:5<513::AID-BIP5>3.0.CO;2-I
    • Tsigelny I., Greenberg J.P., Cox S., Nichols W.L., Taylor S.S., and Ten Eyck L.F. 600 ps molecular dynamics reveals stable substructures and flexible hinge points in cAMP dependent protein kinase Biopolymers 50 1999 513 524 (Pubitemid 29439591)
    • (1999) Biopolymers , vol.50 , Issue.5 , pp. 513-524
    • Tsigelny, I.1    Greenberg, J.P.2    Cox, S.3    Nichols, W.L.4    Taylor, S.S.5    Ten Eyck, L.F.6
  • 26
    • 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., and Ghosh G. Regulation of protein kinases; controlling activity through activation segment conformation Mol. Cell 15 2004 661 675 (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 27
    • 77954626097 scopus 로고    scopus 로고
    • Why an A-loop phospho-mimetic fails to activate PAK1: Understanding an inaccessible kinase state by molecular dynamics simulations
    • Ng Y.W., Raghunathan D., Chan P.M., Baskaran Y., Smith D.J., and Lee C.H. Why an A-loop phospho-mimetic fails to activate PAK1: understanding an inaccessible kinase state by molecular dynamics simulations Structure 18 2010 879 890
    • (2010) Structure , vol.18 , pp. 879-890
    • Ng, Y.W.1    Raghunathan, D.2    Chan, P.M.3    Baskaran, Y.4    Smith, D.J.5    Lee, C.H.6
  • 28
    • 77956627609 scopus 로고    scopus 로고
    • The PP2C-SnRK2 complex: The central regulator of an abscisic acid signalling pathway
    • Hirayama T., and Umezawa T. The PP2C-SnRK2 complex: the central regulator of an abscisic acid signalling pathway Plant Signal. Behav. 5 2010 160 163
    • (2010) Plant Signal. Behav. , vol.5 , pp. 160-163
    • Hirayama, T.1    Umezawa, T.2
  • 29
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., and Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions Protein Eng. 8 1995 127 134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 30
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura N., Zhang X., Endres N.F., Seeliger M.A., Schindler T., and Kuriyan J. Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms Mol. Cell 42 2011 9 22
    • (2011) Mol. Cell , vol.42 , pp. 9-22
    • Jura, N.1    Zhang, X.2    Endres, N.F.3    Seeliger, M.A.4    Schindler, T.5    Kuriyan, J.6
  • 31
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton D.R., Zheng J.H., Eyck L.F., Ashford V.A., Xuong N.H., Taylor S.S., and Sowadski J.M. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414 (Pubitemid 21917165)
    • (1991) Science , vol.253 , Issue.5018 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 32
    • 34247368172 scopus 로고    scopus 로고
    • Lining the pockets of kinases and phosphatases
    • DOI 10.1016/j.sbi.2006.10.006, PII S0959440X06001783, Catalysis and Regulation / Proteins
    • Gold M.G., Barford D., and Komander D. Lining the pockets of kinases and phosphatases Curr. Opin. Struct. Biol. 16 2006 693 701 (Pubitemid 44827729)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.6 , pp. 693-701
    • Gold, M.G.1    Barford, D.2    Komander, D.3
  • 33
    • 0028157664 scopus 로고
    • Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution
    • Zhang F., Strand A., Robbins D., Cobb M.H., and Goldsmith E.J. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution Nature 367 1994 704 711
    • (1994) Nature , vol.367 , pp. 704-711
    • Zhang, F.1    Strand, A.2    Robbins, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 34
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • Biondi R.M., Komander D., Thomas C.C., Lizcano J.M., Deak M., Alessi D.R., and van Aalten D.M. High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site EMBO J. 21 2002 4219 4228
    • (2002) EMBO J. , vol.21 , pp. 4219-4228
    • Biondi, R.M.1    Komander, D.2    Thomas, C.C.3    Lizcano, J.M.4    Deak, M.5    Alessi, D.R.6    Van Aalten, D.M.7
  • 35
    • 21444441749 scopus 로고    scopus 로고
    • Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding
    • DOI 10.1074/jbc.M500977200
    • Komander D., Kular G., Deak M., Alessi D.R., and van Aalten D.M. Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding J. Biol. Chem. 280 2005 18797 18802 (Pubitemid 41379581)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18797-18802
    • Komander, D.1    Kular, G.2    Deak, M.3    Alessi, D.R.4    Van Aalten, D.M.F.5
  • 38
    • 0036999615 scopus 로고    scopus 로고
    • Salt and drought stress signal transduction in plants
    • Zhu J.K. Salt and drought stress signal transduction in plants Annu. Rev. Plant Biol. 53 2002 247 273
    • (2002) Annu. Rev. Plant Biol. , vol.53 , pp. 247-273
    • Zhu, J.K.1
  • 39
    • 0034949516 scopus 로고    scopus 로고
    • Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance
    • DOI 10.1105/tpc.13.6.1383
    • Guo Y., Halfter U., Ishitani M., and Zhu J.K. Molecular characterization of functional domains in the protein kinase SOS2 that is required for salt tolerance Plant Cell. 13 2001 1383 1399 (Pubitemid 32592910)
    • (2001) Plant Cell , vol.13 , Issue.6 , pp. 1383-1399
    • Guo, Y.1    Halfter, U.2    Ishitani, M.3    Zhu, J.-K.4
  • 40
    • 0033738988 scopus 로고    scopus 로고
    • Genetic analysis of plant salt tolerance using Arabidopsis thaliana
    • Zhu J.K. Genetic analysis of plant salt tolerance using Arabidopsis thaliana Plant Physiol. 124 2000 941 948
    • (2000) Plant Physiol. , vol.124 , pp. 941-948
    • Zhu, J.K.1
  • 41
    • 1042290710 scopus 로고    scopus 로고
    • Transgenic Evaluation of Activated Mutant Alleles of SOS2 Reveals a Critical Requirement for Its Kinase Activity and C-Terminal Regulatory Domain for Salt Tolerance in Arabidopsis thaliana
    • DOI 10.1105/tpc.019174
    • Guo Y., Qiu Q.S., Quintero F.J., Pardo J.M., Ohta M., and Zhang C. Transgenic evaluation of activated mutant alleles of SOS2 reveals a critical requirement for its kinase activity and C-terminal regulatory domain for salt tolerance in Arabidopsis thaliana Plant Cell. 16 2004 435 449 (Pubitemid 38192701)
    • (2004) Plant Cell , vol.16 , Issue.2 , pp. 435-449
    • Guo, Y.1    Qiu, Q.-S.2    Quintero, F.J.3    Pardo, J.M.4    Ohta, M.5    Zhang, C.6    Schumaker, K.S.7    Zhu, J.-K.8
  • 42
    • 79957524959 scopus 로고    scopus 로고
    • Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA interactions
    • Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., and Luan S. Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA interactions Mol. Plant 4 2011 527 536
    • (2011) Mol. Plant , vol.4 , pp. 527-536
    • Lan, W.Z.1    Lee, S.C.2    Che, Y.F.3    Jiang, Y.Q.4    Luan, S.5
  • 43
    • 11844292846 scopus 로고    scopus 로고
    • The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response
    • DOI 10.1016/j.jmb.2004.11.025, PII S0022283604014640
    • Sanchez-Barrena M.J., Martinez-Ripoll M., Zhu J.K., and Albert A. The structure of the Arabidopsis thaliana SOS3: molecular mechanism of sensing calcium for salt stress response J. Mol. Biol. 345 2005 1253 1264 (Pubitemid 40092238)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.5 , pp. 1253-1264
    • Sanchez-Barrena, M.J.1    Martinez-Ripoll, M.2    Zhu, J.-K.3    Albert, A.4
  • 44
    • 79952687811 scopus 로고    scopus 로고
    • SnRK2.6/OST1 from Arabidopsis thaliana: Cloning, expression, purification, crystallization and preliminary X-ray analysis of K50N and D160A mutants
    • Yunta C., Mantinez-Ripoll M., and Albert A. SnRK2.6/OST1 from Arabidopsis thaliana: cloning, expression, purification, crystallization and preliminary X-ray analysis of K50N and D160A mutants Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 67 2011 364 368
    • (2011) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.67 , pp. 364-368
    • Yunta, C.1    Mantinez-Ripoll, M.2    Albert, A.3
  • 46
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26 1993 795 800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 47
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • DOI 10.1107/S0907444901012409
    • Vagin A.A., and Isupov M.N. Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps Acta Crystallogr., Sect. D: Biol. Crystallogr. 57 2001 1451 1456 (Pubitemid 36117196)
    • (2001) Acta Crystallographica Section D: Biological Crystallography , vol.57 , Issue.10 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 48
    • 27144548462 scopus 로고    scopus 로고
    • Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1
    • DOI 10.1016/j.bbrc.2005.09.181, PII S0006291X05022059
    • Rudolph M.J., Amadeo G.A., Bai Y., and Tong L. Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1 Biochem. Biophys. Res. Commun. 337 2005 1224 1228 (Pubitemid 41509194)
    • (2005) Biochemical and Biophysical Research Communications , vol.337 , Issue.4 , pp. 1224-1228
    • Rudolph, M.J.1    Amodeo, G.A.2    Bai, Y.3    Tong, L.4
  • 60
    • 1842481270 scopus 로고    scopus 로고
    • Analysis of heterogeneous interactions
    • Cole J.L. Analysis of heterogeneous interactions Methods Enzymol. 384 2004 212 323
    • (2004) Methods Enzymol. , vol.384 , pp. 212-323
    • Cole, J.L.1


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