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Volumn 111, Issue 42, 2014, Pages E4532-E4541

Structural basis of the regulatory mechanism of the plant CIPK family of protein kinases controlling ion homeostasis and abiotic stress

Author keywords

Abiotic stress; Ion transport; Signaling

Indexed keywords

CALCINEURIN B LIKE INTERACTING PROTEIN KINASE 23; CALCINEURIN B LIKE INTERACTING PROTEIN KINASE 24; ION; PROTEIN KINASE; SOS PROTEIN; SOS2 PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ARABIDOPSIS PROTEIN; CIPK23 PROTEIN, ARABIDOPSIS; CYCLIC AMP DEPENDENT PROTEIN KINASE; LITHIUM; PROTEIN BINDING; PROTEIN SERINE THREONINE KINASE; RECOMBINANT PROTEIN; SODIUM; SOS2 PROTEIN, ARABIDOPSIS;

EID: 84908070141     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1407610111     Document Type: Article
Times cited : (92)

References (77)
  • 1
    • 0035282892 scopus 로고    scopus 로고
    • The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases
    • Albrecht V, Ritz O, Linder S, Harter K, Kudla J (2001) The NAF domain defines a novel protein-protein interaction module conserved in Ca2+-regulated kinases. EMBO J 20(5):1051-1063.
    • (2001) EMBO J , vol.20 , Issue.5 , pp. 1051-1063
    • Albrecht, V.1    Ritz, O.2    Linder, S.3    Harter, K.4    Kudla, J.5
  • 2
    • 0033388972 scopus 로고    scopus 로고
    • Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis
    • Shi J, et al. (1999) Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis. Plant Cell 11(12):2393-2405.
    • (1999) Plant Cell , vol.11 , Issue.12 , pp. 2393-2405
    • Shi, J.1
  • 3
    • 84862121474 scopus 로고    scopus 로고
    • Analysis of calcium signaling pathways in plants
    • Batistič O, Kudla J (2012) Analysis of calcium signaling pathways in plants. Biochim Biophys Acta 1820(8):1283-1293.
    • (2012) Biochim Biophys Acta , vol.1820 , Issue.8 , pp. 1283-1293
    • Batistič, O.1    Kudla, J.2
  • 4
    • 84885221459 scopus 로고    scopus 로고
    • Calcium and reactive oxygen species rule the waves of signaling
    • Steinhorst L, Kudla J (2013) Calcium and reactive oxygen species rule the waves of signaling. Plant Physiol 163(2):471-485.
    • (2013) Plant Physiol , vol.163 , Issue.2 , pp. 471-485
    • Steinhorst, L.1    Kudla, J.2
  • 5
    • 0036276574 scopus 로고    scopus 로고
    • Calmodulins and calcineurin B-like proteins: Calcium sensors for specific signal response coupling in plants
    • Luan S, Kudla J, Rodriguez-Concepcion M, Yalovsky S, Gruissem W (2002) Calmodulins and calcineurin B-like proteins: Calcium sensors for specific signal response coupling in plants. Plant Cell 14(Suppl):S389-S400.
    • (2002) Plant Cell , vol.14 , pp. S389-S400
    • Luan, S.1    Kudla, J.2    Rodriguez-Concepcion, M.3    Yalovsky, S.4    Gruissem, W.5
  • 6
    • 0034949516 scopus 로고    scopus 로고
    • Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance
    • Guo Y, Halfter U, Ishitani M, Zhu JK (2001) Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance. Plant Cell 13(6):1383-1400.
    • (2001) Plant Cell , vol.13 , Issue.6 , pp. 1383-1400
    • Guo, Y.1    Halfter, U.2    Ishitani, M.3    Zhu, J.K.4
  • 7
    • 0037062514 scopus 로고    scopus 로고
    • Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3
    • Qiu QS, Guo Y, Dietrich MA, Schumaker KS, Zhu JK (2002) Regulation of SOS1, a plasma membrane Na+/H+ exchanger in Arabidopsis thaliana, by SOS2 and SOS3. Proc Natl Acad Sci USA 99(12):8436-8441.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.12 , pp. 8436-8441
    • Qiu, Q.S.1    Guo, Y.2    Dietrich, M.A.3    Schumaker, K.S.4    Zhu, J.K.5
  • 8
    • 79952298500 scopus 로고    scopus 로고
    • Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain
    • Quintero FJ, et al. (2011) Activation of the plasma membrane Na/H antiporter Salt-Overly-Sensitive 1 (SOS1) by phosphorylation of an auto-inhibitory C-terminal domain. Proc Natl Acad Sci USA 108(6):2611-2616.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.6 , pp. 2611-2616
    • Quintero, F.J.1
  • 9
    • 84869218776 scopus 로고    scopus 로고
    • Structural insights on the plant salt-overly-sensitive 1 (SOS1) Na(+)/H(+) antiporter
    • Núñez-Ramírez R, et al. (2012) Structural insights on the plant salt-overly-sensitive 1 (SOS1) Na(+)/H(+) antiporter. J Mol Biol 424(5):283-294.
    • (2012) J Mol Biol , vol.424 , Issue.5 , pp. 283-294
    • Núñez-Ramírez, R.1
  • 10
    • 34347376108 scopus 로고    scopus 로고
    • Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein
    • Fuglsang AT, et al. (2007) Arabidopsis protein kinase PKS5 inhibits the plasma membrane H+ -ATPase by preventing interaction with 14-3-3 protein. Plant Cell 19(5):1617-1634.
    • (2007) Plant Cell , vol.19 , Issue.5 , pp. 1617-1634
    • Fuglsang, A.T.1
  • 11
    • 35649006020 scopus 로고    scopus 로고
    • A protein phosphorylation/dephosphorylation network regulates a plant potassium channel
    • Lee SC, et al. (2007) A protein phosphorylation/dephosphorylation network regulates a plant potassium channel. Proc Natl Acad Sci USA 104(40):15959-15964.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.40 , pp. 15959-15964
    • Lee, S.C.1
  • 12
    • 33745251949 scopus 로고    scopus 로고
    • A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis
    • Xu J, et al. (2006) A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell 125(7):1347-1360.
    • (2006) Cell , vol.125 , Issue.7 , pp. 1347-1360
    • Xu, J.1
  • 13
    • 84858045447 scopus 로고    scopus 로고
    • Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins
    • Hashimoto K, et al. (2012) Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins. J Biol Chem 287(11):7956-7968.
    • (2012) J Biol Chem , vol.287 , Issue.11 , pp. 7956-7968
    • Hashimoto, K.1
  • 14
    • 70249134972 scopus 로고    scopus 로고
    • CHL1 functions as a nitrate sensor in plants
    • Ho CH, Lin SH, Hu HC, Tsay YF (2009) CHL1 functions as a nitrate sensor in plants. Cell 138(6):1184-1194.
    • (2009) Cell , vol.138 , Issue.6 , pp. 1184-1194
    • Ho, C.H.1    Lin, S.H.2    Hu, H.C.3    Tsay, Y.F.4
  • 15
    • 35449004150 scopus 로고    scopus 로고
    • The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis
    • Kim BG, et al. (2007) The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis. Plant J 52(3):473-484.
    • (2007) Plant J , vol.52 , Issue.3 , pp. 473-484
    • Kim, B.G.1
  • 16
    • 34250621280 scopus 로고    scopus 로고
    • SCABP8/CBL10, a putative calcium sensor, interacts with the protein kinase SOS2 to protect Arabidopsis shoots from salt stress
    • Quan R, et al. (2007) SCABP8/CBL10, a putative calcium sensor, interacts with the protein kinase SOS2 to protect Arabidopsis shoots from salt stress. Plant Cell 19(4):1415-1431.
    • (2007) Plant Cell , vol.19 , Issue.4 , pp. 1415-1431
    • Quan, R.1
  • 17
    • 0033793156 scopus 로고    scopus 로고
    • SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding
    • Ishitani M, et al. (2000) SOS3 function in plant salt tolerance requires N-myristoylation and calcium binding. Plant Cell 12(9):1667-1678.
    • (2000) Plant Cell , vol.12 , Issue.9 , pp. 1667-1678
    • Ishitani, M.1
  • 18
    • 0141593530 scopus 로고    scopus 로고
    • A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2
    • Ohta M, Guo Y, Halfter U, Zhu JK (2003) A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2. Proc Natl Acad Sci USA 100(20):11771-11776.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.20 , pp. 11771-11776
    • Ohta, M.1    Guo, Y.2    Halfter, U.3    Zhu, J.K.4
  • 19
    • 34247627317 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3
    • Sánchez-Barrena MJ, et al. (2007) The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3. Mol Cell 26(3):427-435.
    • (2007) Mol Cell , vol.26 , Issue.3 , pp. 427-435
    • Sánchez-Barrena, M.J.1
  • 20
    • 84875070900 scopus 로고    scopus 로고
    • Structural biology of a major signaling network that regulates plant abiotic stress: The CBL-CIPK mediated pathway
    • Sánchez-Barrena MJ, Martínez-Ripoll M, Albert A (2013) Structural biology of a major signaling network that regulates plant abiotic stress: The CBL-CIPK mediated pathway. Int J Mol Sci 14(3):5734-5749.
    • (2013) Int J Mol Sci , vol.14 , Issue.3 , pp. 5734-5749
    • Sánchez-Barrena, M.J.1    Martínez-Ripoll, M.2    Albert, A.3
  • 21
    • 84863480170 scopus 로고    scopus 로고
    • S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses
    • Batistič O, et al. (2012) S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses. Cell Res 22(7):1155-1168.
    • (2012) Cell Res , vol.22 , Issue.7 , pp. 1155-1168
    • Batistič, O.1
  • 22
    • 0037173054 scopus 로고    scopus 로고
    • Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis
    • Quintero FJ, Ohta M, Shi H, Zhu JK, Pardo JM (2002) Reconstitution in yeast of the Arabidopsis SOS signaling pathway for Na+ homeostasis. Proc Natl Acad Sci USA 99(13):9061-9066.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.13 , pp. 9061-9066
    • Quintero, F.J.1    Ohta, M.2    Shi, H.3    Zhu, J.K.4    Pardo, J.M.5
  • 23
    • 84897440538 scopus 로고    scopus 로고
    • The vacuolar calcium sensors CBL2 and CBL3 affect seed size and embryonic development in Arabidopsis thaliana
    • Eckert C, et al. (2014) The vacuolar calcium sensors CBL2 and CBL3 affect seed size and embryonic development in Arabidopsis thaliana. Plant J 78(1):146-156.
    • (2014) Plant J , vol.78 , Issue.1 , pp. 146-156
    • Eckert, C.1
  • 24
    • 79960127656 scopus 로고    scopus 로고
    • Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex
    • Held K, et al. (2011) Calcium-dependent modulation and plasma membrane targeting of the AKT2 potassium channel by the CBL4/CIPK6 calcium sensor/protein kinase complex. Cell Res 21(7):1116-1130.
    • (2011) Cell Res , vol.21 , Issue.7 , pp. 1116-1130
    • Held, K.1
  • 25
    • 67651122833 scopus 로고    scopus 로고
    • Phosphorylation of SOS3-LIKE CALCIUM BINDING PROTEIN8 by SOS2 protein kinase stabilizes their protein complex and regulates salt tolerance in Arabidopsis
    • Lin H, et al. (2009) Phosphorylation of SOS3-LIKE CALCIUM BINDING PROTEIN8 by SOS2 protein kinase stabilizes their protein complex and regulates salt tolerance in Arabidopsis. Plant Cell 21(5):1607-1619.
    • (2009) Plant Cell , vol.21 , Issue.5 , pp. 1607-1619
    • Lin, H.1
  • 26
    • 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(5):661-675.
    • (2004) Mol Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 27
    • 0037008783 scopus 로고    scopus 로고
    • Biochemical and functional characterization of PKS11, a novel Arabidopsis protein kinase
    • Gong D, Gong Z, Guo Y, Chen X, Zhu JK (2002) Biochemical and functional characterization of PKS11, a novel Arabidopsis protein kinase. J Biol Chem 277(31):28340-28350.
    • (2002) J Biol Chem , vol.277 , Issue.31 , pp. 28340-28350
    • Gong, D.1    Gong, Z.2    Guo, Y.3    Chen, X.4    Zhu, J.K.5
  • 28
    • 0036740915 scopus 로고    scopus 로고
    • Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance
    • Gong D, Guo Y, Jagendorf AT, Zhu JK (2002) Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance. Plant Physiol 130(1):256-264.
    • (2002) Plant Physiol , vol.130 , Issue.1 , pp. 256-264
    • Gong, D.1    Guo, Y.2    Jagendorf, A.T.3    Zhu, J.K.4
  • 29
    • 84867875116 scopus 로고    scopus 로고
    • Expression, purification and analysis of an Arabidopsis recombinant CBL-interacting protein kinase3 (CIPK3) and its constitutively active form
    • Gao P, Kolenovsky A, Cui Y, Cutler AJ, Tsang EW (2012) Expression, purification and analysis of an Arabidopsis recombinant CBL-interacting protein kinase3 (CIPK3) and its constitutively active form. Protein Expr Purif 86(1):45-52.
    • (2012) Protein Expr Purif , vol.86 , Issue.1 , pp. 45-52
    • Gao, P.1    Kolenovsky, A.2    Cui, Y.3    Cutler, A.J.4    Tsang, E.W.5
  • 30
    • 1642465539 scopus 로고    scopus 로고
    • The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis
    • Gong D, Guo Y, Schumaker KS, Zhu JK (2004) The SOS3 family of calcium sensors and SOS2 family of protein kinases in Arabidopsis. Plant Physiol 134(3):919-926.
    • (2004) Plant Physiol , vol.134 , Issue.3 , pp. 919-926
    • Gong, D.1    Guo, Y.2    Schumaker, K.S.3    Zhu, J.K.4
  • 31
    • 67651116950 scopus 로고    scopus 로고
    • An autophosphorylation site of the protein kinase SOS2 is important for salt tolerance in Arabidopsis
    • Fujii H, Zhu JK (2009) An autophosphorylation site of the protein kinase SOS2 is important for salt tolerance in Arabidopsis. Mol Plant 2(1):183-190.
    • (2009) Mol Plant , vol.2 , Issue.1 , pp. 183-190
    • Fujii, H.1    Zhu, J.K.2
  • 32
    • 70450185133 scopus 로고    scopus 로고
    • Plant 14-3-3 proteins catch up with their mammalian orthologs
    • Oecking C, Jaspert N (2009) Plant 14-3-3 proteins catch up with their mammalian orthologs. Curr Opin Plant Biol 12(6):760-765.
    • (2009) Curr Opin Plant Biol , vol.12 , Issue.6 , pp. 760-765
    • Oecking, C.1    Jaspert, N.2
  • 33
    • 84899131292 scopus 로고    scopus 로고
    • Inhibition of the Arabidopsis salt overly sensitive pathway by 14-3-3 proteins
    • Zhou H, et al. (2014) Inhibition of the Arabidopsis salt overly sensitive pathway by 14-3-3 proteins. Plant Cell 26(3):1166-1182.
    • (2014) Plant Cell , vol.26 , Issue.3 , pp. 1166-1182
    • Zhou, H.1
  • 34
    • 84877588949 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics after auxin-stimulated lateral root induction identifies an SNX1 protein phosphorylation site required for growth
    • Zhang H, et al. (2013) Quantitative phosphoproteomics after auxin-stimulated lateral root induction identifies an SNX1 protein phosphorylation site required for growth. Mol Cell Proteomics 12(5):1158-1169.
    • (2013) Mol Cell Proteomics , vol.12 , Issue.5 , pp. 1158-1169
    • Zhang, H.1
  • 35
    • 4043142209 scopus 로고    scopus 로고
    • Consensus-based engineering of protein stability: From intrabodies to thermostable enzymes
    • Steipe B (2004) Consensus-based engineering of protein stability: From intrabodies to thermostable enzymes. Methods Enzymol 388:176-186.
    • (2004) Methods Enzymol , vol.388 , pp. 176-186
    • Steipe, B.1
  • 36
    • 84907358194 scopus 로고    scopus 로고
    • The consensus-based approach for gene/enzyme replacement therapies and crystallization strategies: The case of human alanine-glyoxylate aminotransferase
    • Mesa-Torres N, et al. (2014) The consensus-based approach for gene/enzyme replacement therapies and crystallization strategies: The case of human alanine-glyoxylate aminotransferase. Biochem J 462(3):453-463.
    • (2014) Biochem J , vol.462 , Issue.3 , pp. 453-463
    • Mesa-Torres, N.1
  • 37
    • 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(7250):1146-1149.
    • (2009) Nature , vol.459 , Issue.7250 , pp. 1146-1149
    • Chen, L.1
  • 38
    • 33644833886 scopus 로고    scopus 로고
    • Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family
    • 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(3):477-485.
    • (2006) Structure , vol.14 , Issue.3 , pp. 477-485
    • Nayak, V.1
  • 39
    • 79551594605 scopus 로고    scopus 로고
    • Protein kinases: Evolution of dynamic regulatory proteins
    • Taylor SS, Kornev AP (2011) Protein kinases: Evolution of dynamic regulatory proteins. Trends Biochem Sci 36(2):65-77.
    • (2011) Trends Biochem Sci , vol.36 , Issue.2 , pp. 65-77
    • Taylor, S.S.1    Kornev, A.P.2
  • 40
    • 84886629236 scopus 로고    scopus 로고
    • Deciphering the structural basis of eukaryotic protein kinase regulation
    • Meharena HS, et al. (2013) Deciphering the structural basis of eukaryotic protein kinase regulation. PLoS Biol 11(10):e1001680.
    • (2013) PLoS Biol , vol.11 , Issue.10 , pp. e1001680
    • Meharena, H.S.1
  • 41
    • 0037469146 scopus 로고    scopus 로고
    • Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model?
    • Adams JA (2003) Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model? Biochemistry 42(3):601-607.
    • (2003) Biochemistry , vol.42 , Issue.3 , pp. 601-607
    • Adams, J.A.1
  • 42
    • 79953308071 scopus 로고    scopus 로고
    • Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms
    • Jura N, et al. (2011) Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms. Mol Cell 42(1):9-22.
    • (2011) Mol Cell , vol.42 , Issue.1 , pp. 9-22
    • Jura, N.1
  • 43
    • 0000127673 scopus 로고
    • 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor
    • Zheng J, et al. (1993) 2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor. Acta Crystallogr D Biol Crystallogr 49(Pt 3):362-365.
    • (1993) Acta Crystallogr D Biol Crystallogr , vol.49 , pp. 362-365
    • Zheng, J.1
  • 44
    • 0036830597 scopus 로고    scopus 로고
    • Constitutive activation and transgenic evaluation of the function of an arabidopsis PKS protein kinase
    • Gong D, Zhang C, Chen X, Gong Z, Zhu JK (2002) Constitutive activation and transgenic evaluation of the function of an arabidopsis PKS protein kinase. J Biol Chem 277(44):42088-42096.
    • (2002) J Biol Chem , vol.277 , Issue.44 , pp. 42088-42096
    • Gong, D.1    Zhang, C.2    Chen, X.3    Gong, Z.4    Zhu, J.K.5
  • 45
    • 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(2):149-158.
    • (1996) Cell , vol.85 , Issue.2 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 46
    • 0037436339 scopus 로고    scopus 로고
    • Relibase: Design and development of a database for comprehensive analysis of protein-ligand interactions
    • Hendlich M, Bergner A, Günther J, Klebe G (2003) Relibase: Design and development of a database for comprehensive analysis of protein-ligand interactions. J Mol Biol 326(2):607-620.
    • (2003) J Mol Biol , vol.326 , Issue.2 , pp. 607-620
    • Hendlich, M.1    Bergner, A.2    Günther, J.3    Klebe, G.4
  • 47
    • 39649114328 scopus 로고    scopus 로고
    • The crystal structure of plant-specific calcium-binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14
    • Akaboshi M, et al. (2008) The crystal structure of plant-specific calcium-binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14. J Mol Biol 377(1):246-257.
    • (2008) J Mol Biol , vol.377 , Issue.1 , pp. 246-257
    • Akaboshi, M.1
  • 48
    • 84868156224 scopus 로고    scopus 로고
    • CAVER 3.0: A tool for the analysis of transport pathways in dynamic protein structures
    • Chovancova E, et al. (2012) CAVER 3.0: A tool for the analysis of transport pathways in dynamic protein structures. PLOS Comput Biol 8(10):e1002708.
    • (2012) PLOS Comput Biol , vol.8 , Issue.10 , pp. e1002708
    • Chovancova, E.1
  • 49
    • 0029871290 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I
    • Goldberg J, Nairn AC, Kuriyan J (1996) Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. Cell 84(6):875-887.
    • (1996) Cell , vol.84 , Issue.6 , pp. 875-887
    • Goldberg, J.1    Nairn, A.C.2    Kuriyan, J.3
  • 50
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly SM, Jess TJ, Price NC (2005) How to study proteins by circular dichroism. Biochim Biophys Acta 1751(2):119-139.
    • (2005) Biochim Biophys Acta , vol.1751 , Issue.2 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 51
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases. Biopolymers 89(5):392-400.
    • (2008) Biopolymers , vol.89 , Issue.5 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 52
    • 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(1):135-144.
    • (2011) J Mol Biol , vol.414 , Issue.1 , pp. 135-144
    • Yunta, C.1    Martínez-Ripoll, M.2    Zhu, J.K.3    Albert, A.4
  • 53
    • 84862950886 scopus 로고    scopus 로고
    • Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases
    • Ng LM, et al. (2011) Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases. Proc Natl Acad Sci USA 108(52):21259-21264.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.52 , pp. 21259-21264
    • Ng, L.M.1
  • 54
    • 34247368172 scopus 로고    scopus 로고
    • Lining the pockets of kinases and phosphatases
    • Gold MG, Barford D, Komander D (2006) Lining the pockets of kinases and phosphatases. Curr Opin Struct Biol 16(6):693-701.
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.6 , pp. 693-701
    • Gold, M.G.1    Barford, D.2    Komander, D.3
  • 55
    • 34249105476 scopus 로고    scopus 로고
    • Structural basis for the inhibition of tyrosine kinase activity of ZAP-70
    • Deindl S, et al. (2007) Structural basis for the inhibition of tyrosine kinase activity of ZAP-70. Cell 129(4):735-746.
    • (2007) Cell , vol.129 , Issue.4 , pp. 735-746
    • Deindl, S.1
  • 56
    • 11844292846 scopus 로고    scopus 로고
    • The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response
    • Sánchez-Barrena MJ, Martínez-Ripoll M, Zhu JK, Albert A (2005) The structure of the Arabidopsis thaliana SOS3: Molecular mechanism of sensing calcium for salt stress response. J Mol Biol 345(5):1253-1264.
    • (2005) J Mol Biol , vol.345 , Issue.5 , pp. 1253-1264
    • Sánchez-Barrena, M.J.1    Martínez-Ripoll, M.2    Zhu, J.K.3    Albert, A.4
  • 57
    • 36049031801 scopus 로고    scopus 로고
    • SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity
    • Batelli G, et al. (2007) SOS2 promotes salt tolerance in part by interacting with the vacuolar H+-ATPase and upregulating its transport activity. Mol Cell Biol 27(22):7781-7790.
    • (2007) Mol Cell Biol , vol.27 , Issue.22 , pp. 7781-7790
    • Batelli, G.1
  • 58
    • 0442321060 scopus 로고    scopus 로고
    • The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance
    • Cheng NH, Pittman JK, Zhu JK, Hirschi KD (2004) The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance. J Biol Chem 279(4):2922-2926.
    • (2004) J Biol Chem , vol.279 , Issue.4 , pp. 2922-2926
    • Cheng, N.H.1    Pittman, J.K.2    Zhu, J.K.3    Hirschi, K.D.4
  • 59
    • 0347052888 scopus 로고    scopus 로고
    • Regulation of vacuolar Na+/H+ exchange in Arabidopsis thaliana by the salt-overly-sensitive (SOS) pathway
    • Qiu QS, et al. (2004) Regulation of vacuolar Na+/H+ exchange in Arabidopsis thaliana by the salt-overly-sensitive (SOS) pathway. J Biol Chem 279(1):207-215.
    • (2004) J Biol Chem , vol.279 , Issue.1 , pp. 207-215
    • Qiu, Q.S.1
  • 60
    • 84875581613 scopus 로고    scopus 로고
    • Release of SOS2 kinase from sequestration with GIGANTEA determines salt tolerance in Arabidopsis
    • Kim WY, et al. (2013) Release of SOS2 kinase from sequestration with GIGANTEA determines salt tolerance in Arabidopsis. Nat Commun 4:1352.
    • (2013) Nat Commun , vol.4 , pp. 1352
    • Kim, W.Y.1
  • 61
    • 36048982154 scopus 로고    scopus 로고
    • Interaction of SOS2 with nucleoside diphosphate kinase 2 and catalases reveals a point of connection between salt stress and H2O2 signaling in Arabidopsis thaliana
    • Verslues PE, et al. (2007) Interaction of SOS2 with nucleoside diphosphate kinase 2 and catalases reveals a point of connection between salt stress and H2O2 signaling in Arabidopsis thaliana. Mol Cell Biol 27(22):7771-7780.
    • (2007) Mol Cell Biol , vol.27 , Issue.22 , pp. 7771-7780
    • Verslues, P.E.1
  • 62
    • 0027182508 scopus 로고
    • Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast
    • Mitchell DA, Marshall TK, Deschenes RJ (1993) Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeast 9(7):715-722.
    • (1993) Yeast , vol.9 , Issue.7 , pp. 715-722
    • Mitchell, D.A.1    Marshall, T.K.2    Deschenes, R.J.3
  • 65
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62(Pt 1):72-82.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 72-82
    • Evans, P.1
  • 66
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin AA, Isupov MN (2001) Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr D Biol Crystallogr 57(Pt 10):1451-1456.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 67
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 68
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov GN, et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67(Pt 4):355-367.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 355-367
    • Murshudov, G.N.1
  • 69
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 70
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Anonymous; Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
    • Anonymous1
  • 71
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 73
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • Lietha D, et al. (2007) Structural basis for the autoinhibition of focal adhesion kinase. Cell 129(6):1177-1187.
    • (2007) Cell , vol.129 , Issue.6 , pp. 1177-1187
    • Lietha, D.1
  • 74
    • 0033610850 scopus 로고    scopus 로고
    • Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue
    • LaFevre-Bernt M, et al. (1998) Intramolecular regulatory interactions in the Src family kinase Hck probed by mutagenesis of a conserved tryptophan residue. J Biol Chem 273(48):32129-32134.
    • (1998) J Biol Chem , vol.273 , Issue.48 , pp. 32129-32134
    • LaFevre-Bernt, M.1
  • 75
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees JG, Miles AJ, Wien F, Wallace BA (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22(16):1955-1962.
    • (2006) Bioinformatics , vol.22 , Issue.16 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 76
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • Lobley A, Whitmore L, Wallace BA (2002) DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18(1):211-212.
    • (2002) Bioinformatics , vol.18 , Issue.1 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 77
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet P, Courcelle E, Stuart DI, Métoz F (1999) ESPript: Analysis of multiple sequence alignments in PostScript. Bioinformatics 15(4):305-308.
    • (1999) Bioinformatics , vol.15 , Issue.4 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4


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