메뉴 건너뛰기




Volumn 26, Issue 12, 2014, Pages 4802-4820

C2-domain abscisic acid-related proteins mediate the interaction of PYR/PYL/RCAR abscisic acid receptors with the plasma membrane and regulate abscisic acid sensitivity in arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 84922198487     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.114.129973     Document Type: Article
Times cited : (125)

References (84)
  • 3
    • 78650627501 scopus 로고    scopus 로고
    • Membrane docking of the C2 domain from protein kinase Ca as seen by polarized ATR-IR. The role of PIP2. Bio- chim. Biophys
    • Ausili, A., Corbalan-Garcia, S., Gomez-Fernandez, J.C., and Marsh, D. (2011). Membrane docking of the C2 domain from protein kinase Ca as seen by polarized ATR-IR. The role of PIP2. Bio- chim. Biophys. Acta 1808: 684-695.
    • (2011) Acta , vol.1808 , pp. 684-695
    • Ausili, A.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Marsh, D.4
  • 4
    • 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
    • Batistic, O., Rehers, M., Akerman, A., Schlucking, K., Steinhorst, L., Yalovsky, S., and Kudla, J. (2012). S-Acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses. Cell Res. 22: 1155-1168.
    • (2012) Cell Res , vol.22 , pp. 1155-1168
    • Batistic, O.1    Rehers, M.2    Akerman, A.3    Schlucking, K.4    Steinhorst, L.5    Yalovsky, S.6    Kudla, J.7
  • 5
    • 73849141867 scopus 로고    scopus 로고
    • CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores
    • Batistic, O., Waadt, R., Steinhorst, L., Held, K., and Kudla, J. (2010). CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores. Plant J. 61: 211-222.
    • (2010) Plant J , vol.61 , pp. 211-222
    • Batistic, O.1    Waadt, R.2    Steinhorst, L.3    Held, K.4    Kudla, J.5
  • 7
    • 1542328221 scopus 로고    scopus 로고
    • Analysis of an activated ABI5 allele using a new selection method for transgenic Arabidopsis seeds
    • Bensmihen, S., To, A., Lambert, G., Kroj, T., Giraudat, J., and Parcy, F. (2004). Analysis of an activated ABI5 allele using a new selection method for transgenic Arabidopsis seeds. FEBS Lett. 561: 127-131.
    • (2004) FEBS Lett , vol.561 , pp. 127-131
    • Bensmihen, S.1    To, A.2    Lambert, G.3    Kroj, T.4    Giraudat, J.5    Parcy, F.6
  • 9
    • 84881187701 scopus 로고    scopus 로고
    • An ABA-mimicking ligand that reduces water loss and promotes drought resistance in plants
    • Cao, M., et al. (2013). An ABA-mimicking ligand that reduces water loss and promotes drought resistance in plants. Cell Res. 23: 10431054.
    • (2013) Cell Res , vol.23 , Issue.1043
    • Cao, M.1
  • 10
    • 84885206709 scopus 로고    scopus 로고
    • Nuclear calcium signaling in plants
    • Charpentier, M., and Oldroyd, G.E. (2013). Nuclear calcium signaling in plants. Plant Physiol. 163: 496-503.
    • (2013) Plant Physiol , vol.163 , pp. 496-503
    • Charpentier, M.1    Oldroyd, G.E.2
  • 11
    • 0036016443 scopus 로고    scopus 로고
    • Physical and functional interaction of the Arabidopsis K+ channel AKT2 and phosphatase AtPP2CA
    • Cherel, I., Michard, E., Platet, N., Mouline, K., Alcon, C., Sentenac, H., and Thibaud, J.B. (2002). Physical and functional interaction of the Arabidopsis K+ channel AKT2 and phosphatase AtPP2CA. Plant Cell 14: 1133-1146.
    • (2002) Plant Cell , vol.14 , pp. 1133-1146
    • Cherel, I.1    Michard, E.2    Platet, N.3    Mouline, K.4    Alcon, C.5    Sentenac, H.6    Thibaud, J.B.7
  • 12
    • 0035884406 scopus 로고    scopus 로고
    • Membrane binding assays for peripheral proteins. Anal
    • Cho, W., Bittova, L., and Stahelin, R.V. (2001). Membrane binding assays for peripheral proteins. Anal. Biochem. 296: 153-161.
    • (2001) Biochem , vol.296 , pp. 153-161
    • Cho, W.1    Bittova, L.2    Stahelin, R.V.3
  • 13
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • Cho, W., and Stahelin, R.V. (2005). Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Bio- mol. Struct. 34: 119-151.
    • (2005) Annu. Rev. Biophys. Bio- mol. Struct , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 14
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and sub- cellular targeting of C2 domains. Biochim. Biophys
    • Cho, W., and Stahelin, R.V. (2006). Membrane binding and sub- cellular targeting of C2 domains. Biochim. Biophys. Acta 1761: 838849.
    • (2006) Acta , vol.1761 , Issue.89
    • Cho, W.1    Stahelin, R.V.2
  • 15
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (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
  • 17
    • 0032563217 scopus 로고    scopus 로고
    • Calcium- dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synapto- tagmin binds membranes electrostatically
    • Davletov, B., Perisic, O., and Williams, R.L. (1998). Calcium- dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synapto- tagmin binds membranes electrostatically. J. Biol. Chem. 273: 19093-19096.
    • (1998) J. Biol. Chem , vol.273 , pp. 19093-19096
    • Davletov, B.1    Perisic, O.2    Williams, R.L.3
  • 20
    • 83055178883 scopus 로고    scopus 로고
    • Crystallization and preliminary crystal- lographic analysis of a C2 protein from Arabidopsis thaliana. Acta Crystallogr
    • Diaz, M., Rodriguez, L., Gonzalez-Guzman, M., Martinez-Ripoll, M., and Albert, A. (2011). Crystallization and preliminary crystal- lographic analysis of a C2 protein from Arabidopsis thaliana. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67: 1575-1578.
    • (2011) Sect. F Struct. Biol. Cryst. Commun , vol.67 , pp. 1575-1578
    • Diaz, M.1    Rodriguez, L.2    Gonzalez-Guzman, M.3    Martinez-Ripoll, M.4    Albert, A.5
  • 21
    • 77952530584 scopus 로고    scopus 로고
    • The language of calcium signaling. Annu
    • Dodd, A.N., Kudla, J., and Sanders, D. (2010). The language of calcium signaling. Annu. Rev. Plant Biol. 61: 593-620.
    • (2010) Rev. Plant Biol , vol.61 , pp. 593-620
    • Dodd, A.N.1    Kudla, J.2    Sanders, D.3
  • 22
    • 84874520026 scopus 로고    scopus 로고
    • Endodermal ABA signaling promotes lateral root quiescence during salt stress in Arabidopsis seedlings
    • Duan, L., Dietrich, D., Ng, C.H., Chan, P.M., Bhalerao, R., Bennett, M.J., and Dinneny, J.R. (2013). Endodermal ABA signaling promotes lateral root quiescence during salt stress in Arabidopsis seedlings. Plant Cell 25: 324-341.
    • (2013) Plant Cell , vol.25 , pp. 324-341
    • Duan, L.1    Dietrich, D.2    Ng, C.H.3    Chan, P.M.4    Bhalerao, R.5    Bennett, M.J.6    Dinneny, J.R.7
  • 24
    • 80054890183 scopus 로고    scopus 로고
    • A thermodynamic switch modulates abscisic acid receptor sensitivity
    • Dupeux, F., et al. (2011b). A thermodynamic switch modulates abscisic acid receptor sensitivity. EMBO J. 30: 4171-4184.
    • (2011) EMBO J , vol.30 , pp. 4171-4184
    • Dupeux, F.1
  • 25
    • 0037435606 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling
    • Frazier, A.A., Roller, C.R., Havelka, J.J., Hinderliter, A., and Cafiso, D.S. (2003). Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling. Biochemistry 42: 96-105.
    • (2003) Biochemistry , vol.42 , pp. 96-105
    • Frazier, A.A.1    Roller, C.R.2    Havelka, J.J.3    Hinderliter, A.4    Cafiso, D.S.5
  • 26
    • 42049116064 scopus 로고    scopus 로고
    • Colocalization of fluorescent markers in confocal microscope images of plant cells. Nat
    • French, A.P., Mills, S., Swarup, R., Bennett, M.J., and Pridmore, T.P. (2008). Colocalization of fluorescent markers in confocal microscope images of plant cells. Nat. Protoc. 3: 619-628.
    • (2008) Protoc , vol.3 , pp. 619-628
    • French, A.P.1    Mills, S.2    Swarup, R.3    Bennett, M.J.4    Pridmore, T.P.5
  • 27
    • 77955148079 scopus 로고    scopus 로고
    • Calcium-regulated transcription in plants. Mol
    • Galon, Y., Finkler, A., and Fromm, H. (2010). Calcium-regulated transcription in plants. Mol. Plant 3: 653-669.
    • (2010) Plant , vol.3 , pp. 653-669
    • Galon, Y.1    Finkler, A.2    Fromm, H.3
  • 32
    • 84884614907 scopus 로고    scopus 로고
    • A nuclear calcium-sensing pathway is critical for gene regulation and salt stress tolerance in Arabidopsis
    • Guan, Q., Wu, J., Yue, X., Zhang, Y., and Zhu, J. (2013). A nuclear calcium-sensing pathway is critical for gene regulation and salt stress tolerance in Arabidopsis. PLoS Genet. 9: e1003755.
    • (2013) PLoS Genet , pp. 9
    • Guan, Q.1    Wu, J.2    Yue, X.3    Zhang, Y.4    Zhu, J.5
  • 34
    • 34447647309 scopus 로고    scopus 로고
    • The C2 domains of classical PKCs are specific PtdIns(4,5)P2-sensing domains with different affinities for membrane binding
    • Guerrero-Valero, M., Marm-Vicente, C., Gomez-Fernandez, J.C., and Corbalan-Garcfa, S. (2007). The C2 domains of classical PKCs are specific PtdIns(4,5)P2-sensing domains with different affinities for membrane binding. J. Mol. Biol. 371: 608-621.
    • (2007) J. Mol. Biol , vol.371 , pp. 608-621
    • Guerrero-Valero, M.1    Marm-Vicente, C.2    Gomez-Fernandez, J.C.3    Corbalan-Garcfa, S.4
  • 35
    • 0036696407 scopus 로고    scopus 로고
    • A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis. Dev
    • Guo, Y., Xiong, L., Song, C.P., Gong, D., Halfter, U., and Zhu, J.K. (2002). A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis. Dev. Cell 3: 233-244.
    • (2002) Cell , vol.3 , pp. 233-244
    • Guo, Y.1    Xiong, L.2    Song, C.P.3    Gong, D.4    Halfter, U.5    Zhu, J.K.6
  • 36
    • 79958076387 scopus 로고    scopus 로고
    • The molecular basis of ABA- independent inhibition of PP2Cs by a subclass of PYL proteins. Mol
    • Hao, Q., Yin, P., Li, W., Wang, L., Yan, C., Lin, Z., Wu, J.Z., Wang, J., Yan, S.F., and Yan, N. (2011). The molecular basis of ABA- independent inhibition of PP2Cs by a subclass of PYL proteins. Mol. Cell 42: 662-672.
    • (2011) Cell , vol.42 , pp. 662-672
    • Hao, Q.1    Yin, P.2    Li, W.3    Wang, L.4    Yan, C.5    Lin, Z.6    Wu, J.Z.7    Wang, J.8    Yan, S.F.9    Yan, N.10
  • 37
    • 77955885246 scopus 로고    scopus 로고
    • Early abscisic acid signal transduction mechanisms: Newly discovered components and newly emerging questions
    • Hubbard, K.E., Nishimura, N., Hitomi, K., Getzoff, E.D., and Schroeder, J.I. (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
  • 38
    • 33750989900 scopus 로고    scopus 로고
    • Rapid transcriptome changes induced by cytosolic Ca2+ transients reveal ABRE-related sequences as Ca2+-responsive cis elements in Arabidopsis
    • Kaplan, B., Davydov, O., Knight, H., Galon, Y., Knight, M.R., Fluhr, R., and Fromm, H. (2006). Rapid transcriptome changes induced by cytosolic Ca2+ transients reveal ABRE-related sequences as Ca2+-responsive cis elements in Arabidopsis. Plant Cell 18:2733-2748.
    • (2006) Plant Cell , vol.18 , pp. 2733-2748
    • Kaplan, B.1    Davydov, O.2    Knight, H.3    Galon, Y.4    Knight, M.R.5    Fluhr, R.6    Fromm, H.7
  • 39
    • 0033884980 scopus 로고    scopus 로고
    • Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root
    • Kiegle, E., Moore, C.A., Haseloff, J., Tester, M.A., and Knight, M.R. (2000). Cell-type-specific calcium responses to drought, salt and cold in the Arabidopsis root. Plant J. 23: 267-278.
    • (2000) Plant J , vol.23 , pp. 267-278
    • Kiegle, E.1    Moore, C.A.2    Haseloff, J.3    Tester, M.A.4    Knight, M.R.5
  • 40
    • 34247200577 scopus 로고    scopus 로고
    • The AtGenExpress global stress expression data set: Protocols, evaluation and model data analysis of UV-B light, drought and cold stress responses
    • Kilian, J., Whitehead, D., Horak, J., Wanke, D., Weinl, S., Batistic, O., D’Angelo, C., Bornberg-Bauer, E., Kudla, J., and Harter, K. (2007). The AtGenExpress global stress expression data set: Protocols, evaluation and model data analysis of UV-B light, drought and cold stress responses. Plant J. 50: 347-363.
    • (2007) Plant J , vol.50 , pp. 347-363
    • Kilian, J.1    Whitehead, D.2    Horak, J.3    Wanke, D.4    Weinl, S.5    Batistic, O.6    D’angelo, C.7    Bornberg-Bauer, E.8    Kudla, J.9    Harter, K.10
  • 41
    • 10744220812 scopus 로고    scopus 로고
    • Rice C2-domain proteins are induced and translocated to the plasma membrane in response to a fungal elicitor
    • Kim, C.Y., et al. (2003). Rice C2-domain proteins are induced and translocated to the plasma membrane in response to a fungal elicitor. Biochemistry 42: 11625-11633.
    • (2003) Biochemistry , vol.42 , pp. 11625-11633
    • Kim, C.Y.1
  • 42
    • 77952466564 scopus 로고    scopus 로고
    • Guard cell signal transduction network: Advances in understanding abscisic acid, CO2, and Ca2+ signaling. Annu
    • Kim, T.H., Bohmer, M., Hu, H., Nishimura, N., and Schroeder, J.I. (2010). Guard cell signal transduction network: Advances in understanding abscisic acid, CO2, and Ca2+ signaling. Annu. Rev. Plant Biol. 61: 561-591.
    • (2010) Rev. Plant Biol , vol.61 , pp. 561-591
    • Kim, T.H.1    Bohmer, M.2    Hu, H.3    Nishimura, N.4    Schroeder, J.I.5
  • 43
    • 0347298574 scopus 로고    scopus 로고
    • C2 domain of protein kinase C alpha: Elucidation of the membrane docking surface by site-directed fluorescence and spin labeling
    • Kohout, S.C., Corbalan-Garcia, S., Gomez-Fernandez, J.C., and Falke, J.J. (2003). C2 domain of protein kinase C alpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry 42: 1254-1265.
    • (2003) Biochemistry , vol.42 , pp. 1254-1265
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Falke, J.J.4
  • 44
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol
    • Krissinel, E., and Henrick, K. (2004). Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60: 2256-2268.
    • (2004) Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 45
    • 78549267766 scopus 로고    scopus 로고
    • The structural basis for membrane binding and pore formation by lymphocyte perforin
    • Law, R.H., et al. (2010). The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature 468: 447-451.
    • (2010) Nature , vol.468 , pp. 447-451
    • Law, R.H.1
  • 46
    • 75849136096 scopus 로고    scopus 로고
    • A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells
    • Lee, S.C., Lan, W., Buchanan, B.B., and Luan, S. (2009). A protein kinase-phosphatase pair interacts with an ion channel to regulate ABA signaling in plant guard cells. Proc. Natl. Acad. Sci. USA 106: 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
  • 48
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M.A. (2008). Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 9: 99-111.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 49
    • 84870237345 scopus 로고    scopus 로고
    • Direct interactions of ABA-insensitive (ABI)-clade protein phosphatase (PP) 2Cs with calcium-dependent protein kinases and ABA response element-binding bZIPs may contribute to turning off ABA response. Plant Mol
    • Lynch, T., Erickson, B.J., and Finkelstein, R.R. (2012). Direct interactions of ABA-insensitive (ABI)-clade protein phosphatase (PP) 2Cs with calcium-dependent protein kinases and ABA response element-binding bZIPs may contribute to turning off ABA response. Plant Mol. Biol. 80: 647-658.
    • (2012) Biol , vol.80 , pp. 647-658
    • Lynch, T.1    Erickson, B.J.2    Finkelstein, R.R.3
  • 50
    • 84879918048 scopus 로고    scopus 로고
    • Arabidopsis CIPK26 interacts with KEG, components of the ABA signalling network and is degraded by the ubiquitin-proteasome system
    • Lyzenga, W.J., Liu, H., Schofield, A., Muise-Hennessey, A., and Stone, S.L. (2013). Arabidopsis CIPK26 interacts with KEG, components of the ABA signalling network and is degraded by the ubiquitin-proteasome system. J. Exp. Bot. 64: 2779-2791.
    • (2013) J. Exp. Bot , vol.64 , pp. 2779-2791
    • Lyzenga, W.J.1    Liu, H.2    Schofield, A.3    Muise-Hennessey, A.4    Stone, S.L.5
  • 51
    • 66249133969 scopus 로고    scopus 로고
    • Regulators of PP2C phosphatase activity function as abscisic acid sensors
    • Ma, Y., Szostkiewicz, I., Korte, A., Moes, D., Yang, Y., Christmann, A., and Grill, E. (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    Szostkiewicz, I.2    Korte, A.3    Moes, D.4    Yang, Y.5    Christmann, A.6    Grill, E.7
  • 52
    • 57649171349 scopus 로고    scopus 로고
    • Shaping the calcium signature
    • McAinsh, M.R., and Pittman, J.K. (2009). Shaping the calcium signature. New Phytol. 181: 275-294.
    • (2009) New Phytol , vol.181 , pp. 275-294
    • Mc ainsh, M.R.1    Pittman, J.K.2
  • 53
    • 0032492686 scopus 로고    scopus 로고
    • Differential membrane-binding and activation mechanisms of protein kinase C-alpha and -epsilon
    • Medkova, M., and Cho, W. (1998). Differential membrane-binding and activation mechanisms of protein kinase C-alpha and -epsilon. Biochemistry 37: 4892-4900.
    • (1998) Biochemistry , vol.37 , pp. 4892-4900
    • Medkova, M.1    Cho, W.2
  • 54
    • 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
  • 55
    • 84890246880 scopus 로고    scopus 로고
    • A Nobel Prize for membrane traffic: Vesicles find their journey's end
    • Mellman, I., and Emr, S.D. (2013). A Nobel Prize for membrane traffic: Vesicles find their journey's end. J. Cell Biol. 203: 559-561.
    • (2013) J. Cell Biol , vol.203 , pp. 559-561
    • Mellman, I.1    Emr, S.D.2
  • 56
    • 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
  • 58
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka, Y. (1988). The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334: 661 -665.
    • (1988) Nature 334: 661 -665
    • Nishizuka, Y.1
  • 60
    • 66249110335 scopus 로고    scopus 로고
    • Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins
    • Park, S.Y., 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
  • 61
    • 0031892519 scopus 로고    scopus 로고
    • Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2
    • Perisic, O., Fong, S., Lynch, D.E., Bycroft, M., and Williams, R.L. (1998). Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273: 1596-1604.
    • (1998) J. Biol. Chem , vol.273 , pp. 1596-1604
    • Perisic, O.1    Fong, S.2    Lynch, D.E.3    Bycroft, M.4    Williams, R.L.5
  • 62
    • 84883255166 scopus 로고    scopus 로고
    • The PYL4 A194T mutant uncovers a key role of PYR1-LIKE4/ PROTEIN PHOSPHATASE 2CA interaction for abscisic acid signaling and plant drought resistance
    • Pizzio, G.A., Rodriguez, L., Antoni, R., Gonzalez-Guzman, M., Yunta, C., Merilo, E., Kollist, H., Albert, A., and Rodriguez, P.L. (2013). The PYL4 A194T mutant uncovers a key role of PYR1-LIKE4/ PROTEIN PHOSPHATASE 2CA interaction for abscisic acid signaling and plant drought resistance. Plant Physiol. 163: 441-455.
    • (2013) Plant Physiol , vol.163 , pp. 441-455
    • Pizzio, G.A.1    Rodriguez, L.2    Antoni, R.3    Gonzalez-Guzman, M.4    Yunta, C.5    Merilo, E.6    Kollist, H.7    Albert, A.8    Rodriguez, P.L.9
  • 63
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, structure and function of a universal Ca2+-binding domain
    • Rizo, J., and Sudhof, T.C. (1998). C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273: 1587915882.
    • (1998) J. Biol. Chem , vol.273 , Issue.158
    • Rizo, J.1    Sudhof, T.C.2
  • 64
    • 84888427451 scopus 로고    scopus 로고
    • ABI1 and PP2CA phosphatases are negative regulators of Snf1-related protein kinase1 signaling in Arabidopsis
    • Rodrigues, A., et al. (2013). ABI1 and PP2CA phosphatases are negative regulators of Snf1-related protein kinase1 signaling in Arabidopsis. Plant Cell 25: 3871-3884.
    • (2013) Plant Cell , vol.25 , pp. 3871-3884
    • Rodrigues, A.1
  • 65
    • 33747085500 scopus 로고    scopus 로고
    • Enhancement of abscisic acid sensitivity and reduction of water consumption in Arabidopsis by combined inactivation of the protein phosphatases type 2C ABI1 and HAB1
    • Saez, A., Robert, N., Maktabi, M.H., Schroeder, J.I., Serrano, R., and Rodriguez, P.L. (2006). Enhancement of abscisic acid sensitivity and reduction of water consumption in Arabidopsis by combined inactivation of the protein phosphatases type 2C ABI1 and HAB1. Plant Physiol. 141: 1389-1399.
    • (2006) Plant Physiol , vol.141 , pp. 1389-1399
    • Saez, A.1    Robert, N.2    Maktabi, M.H.3    Schroeder, J.I.4    Serrano, R.5    Rodriguez, P.L.6
  • 66
    • 58549100260 scopus 로고    scopus 로고
    • HAB1-SWI3B interaction reveals a link between abscisic acid signaling and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis
    • Saez, A., Rodrigues, A., Santiago, J., Rubio, S., and Rodriguez, P.L. (2008). HAB1-SWI3B interaction reveals a link between abscisic acid signaling and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis. Plant Cell 20: 2972-2988.
    • (2008) Plant Cell , vol.20 , pp. 2972-2988
    • Saez, A.1    Rodrigues, A.2    Santiago, J.3    Rubio, S.4    Rodriguez, P.L.5
  • 68
    • 73149112823 scopus 로고    scopus 로고
    • Threonine at position 306 of theKAT1 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., Shinozaki, K., Hibi, T., Taniguchi, M., Miyake, H., Goto, D.B., and Uozumi, N. (2009). 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: 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    Hibi, T.7    Taniguchi, M.8    Miyake, H.9    Goto, D.B.10    Uozumi, N.11
  • 70
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: Where proteins come together and when they're apart
    • Scott, J.D., and Pawson, T. (2009). Cell signaling in space and time: Where proteins come together and when they're apart. Science 326: 1220-1224.
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 71
  • 73
    • 79955580424 scopus 로고    scopus 로고
    • In vivo imaging of Ca2+, pH, and reactive oxygen species using fluorescent probes in plants. Annu
    • Swanson, S.J., Choi, W.G., Chanoca, A., and Gilroy, S. (2011). In vivo imaging of Ca2+, pH, and reactive oxygen species using fluorescent probes in plants. Annu. Rev. Plant Biol. 62: 273-297.
    • (2011) Rev. Plant Biol , vol.62 , pp. 273-297
    • Swanson, S.J.1    Choi, W.G.2    Chanoca, A.3    Gilroy, S.4
  • 74
    • 0033571223 scopus 로고    scopus 로고
    • Ca2+ bridges the C2 membrane- binding domain of protein kinase Calpha directly to phosphati- dylserine
    • Verdaguer, N., Corbalan-Garcia, S., Ochoa, W.F., Fita, I., and Gomez-Fernandez, J.C. (1999). Ca2+ bridges the C2 membrane- binding domain of protein kinase Calpha directly to phosphati- dylserine. EMBO J. 18: 6329-6338.
    • (1999) EMBO J , vol.18 , pp. 6329-6338
    • Verdaguer, N.1    Corbalan-Garcia, S.2    Ochoa, W.F.3    Fita, I.4    Gomez-Fernandez, J.C.5
  • 77
    • 0037342553 scopus 로고    scopus 로고
    • An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus
    • Voinnet, O., Rivas, S., Mestre, P., and Baulcombe, D. (2003). An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus. Plant J. 33: 949-956.
    • (2003) Plant J , vol.33 , pp. 949-956
    • Voinnet, O.1    Rivas, S.2    Mestre, P.3    Baulcombe, D.4
  • 78
    • 54349105689 scopus 로고    scopus 로고
    • Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta
    • Waadt, R., Schmidt, L.K., Lohse, M., Hashimoto, K., Bock, R., and Kudla, J. (2008). Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta. Plant J. 56: 505-516.
    • (2008) Plant J , vol.56 , pp. 505-516
    • Waadt, R.1    Schmidt, L.K.2    Lohse, M.3    Hashimoto, K.4    Bock, R.5    Kudla, J.6
  • 80
    • 67649348445 scopus 로고    scopus 로고
    • Characterization of a canola C2 domain gene that interacts with PG, an effector of the necrotrophic fungus Sclerotinia sclerotiorum
    • Wang, X., Li, Q., Niu, X., Chen, H., Xu, L., and Qi, C. (2009). Characterization of a canola C2 domain gene that interacts with PG, an effector of the necrotrophic fungus Sclerotinia sclerotiorum. J. Exp. Bot. 60: 2613-2620.
    • (2009) J. Exp. Bot , vol.60 , pp. 2613-2620
    • Wang, X.1    Li, Q.2    Niu, X.3    Chen, H.4    Xu, L.5    Qi, C.6
  • 81
    • 62549127319 scopus 로고    scopus 로고
    • Calcium-dependent freezing tolerance in Arabidopsis involves membrane resealing via synaptotagmin SYT1
    • Yamazaki, T., Kawamura, Y., Minami, A., and Uemura, M. (2008). Calcium-dependent freezing tolerance in Arabidopsis involves membrane resealing via synaptotagmin SYT1. Plant Cell 20: 3389-3404.
    • (2008) Plant Cell , vol.20 , pp. 3389-3404
    • Yamazaki, T.1    Kawamura, Y.2    Minami, A.3    Uemura, M.4
  • 82
    • 70350247905 scopus 로고    scopus 로고
    • Overexpression of a rice gene encoding a small C2 domain protein OsSMCP1 increases tolerance to abiotic and biotic stresses in transgenic Arabidopsis. Plant Mol
    • Yokotani, N., Ichikawa, T., Kondou, Y., Maeda, S., Iwabuchi, M., Mori, M., Hirochika, H., Matsui, M., and Oda, K. (2009). Overexpression of a rice gene encoding a small C2 domain protein OsSMCP1 increases tolerance to abiotic and biotic stresses in transgenic Arabidopsis. Plant Mol. Biol. 71: 391-402.
    • (2009) Biol , vol.71 , pp. 391-402
    • Yokotani, N.1    Ichikawa, T.2    Kondou, Y.3    Maeda, S.4    Iwabuchi, M.5    Mori, M.6    Hirochika, H.7    Matsui, M.8    Oda, K.9
  • 83
    • 33646540385 scopus 로고    scopus 로고
    • CO2 signaling in guard cells: Calcium sensitivity response modulation, a Ca2+-independent phase, and CO2 insensitivity of the gca2 mutant
    • Young, J.J., Mehta, S., Israelsson, M., Godoski, J., Grill, E., and Schroeder, J.I. (2006). CO2 signaling in guard cells: Calcium sensitivity response modulation, a Ca2+-independent phase, and CO2 insensitivity of the gca2 mutant. Proc. Natl. Acad. Sci. USA 103: 7506-7511.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7506-7511
    • Young, J.J.1    Mehta, S.2    Israelsson, M.3    Godoski, J.4    Grill, E.5    Schroeder, J.I.6
  • 84
    • 77957866592 scopus 로고    scopus 로고
    • Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes
    • Zhang, D., and Aravind, L. (2010). Identification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotes. Gene 469: 18-30.
    • (2010) Gene , vol.469 , pp. 18-30
    • Zhang, D.1    Aravind, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.