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Volumn 7, Issue 2, 2012, Pages

Subcellular localization of class II HDAs in Arabidopsis thaliana: Nucleocytoplasmic shuttling of HDA15 is driven by light

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; HISTONE DEACETYLASE 14; HISTONE DEACETYLASE 15; HISTONE DEACETYLASE 2; HISTONE DEACETYLASE 5; HISTONE DEACETYLASE 8; HYDROLASE; MESSENGER RNA; PROTEIN 14 3 3; UNCLASSIFIED DRUG; ARABIDOPSIS PROTEIN; GREEN FLUORESCENT PROTEIN; HDA15 PROTEIN, ARABIDOPSIS; HYBRID PROTEIN;

EID: 84857184332     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030846     Document Type: Article
Times cited : (52)

References (89)
  • 1
    • 0036929765 scopus 로고    scopus 로고
    • Analysis of histone acetyltransferases and histone deacetylase families in Arabidopsis thaliana suggests functional diversification of chromatin modifications among multicellular eukaryotes
    • Pandey R, Muller A, Napoli C, Selinger D, Pikaard C, et al. (2002) Analysis of histone acetyltransferases and histone deacetylase families in Arabidopsis thaliana suggests functional diversification of chromatin modifications among multicellular eukaryotes. Nuc Acid Res 30: 5036-5055.
    • (2002) Nuc Acid Res , vol.30 , pp. 5036-5055
    • Pandey, R.1    Muller, A.2    Napoli, C.3    Selinger, D.4    Pikaard, C.5
  • 2
    • 0034057586 scopus 로고    scopus 로고
    • Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana
    • Wu K, Tian L, Malik K, Brown D, Miki B, (2000) Functional analysis of HD2 histone deacetylase homologues in Arabidopsis thaliana. Plant J 22: 19-27.
    • (2000) Plant J , vol.22 , pp. 19-27
    • Wu, K.1    Tian, L.2    Malik, K.3    Brown, D.4    Miki, B.5
  • 3
    • 48249157844 scopus 로고    scopus 로고
    • Histone deacetylase genes in Arabidopsis development
    • Hollender C, Lui Z, (2008) Histone deacetylase genes in Arabidopsis development. J Integ Plant Biol 50: 875-885.
    • (2008) J Integ Plant Biol , vol.50 , pp. 875-885
    • Hollender, C.1    Lui, Z.2
  • 4
    • 65349160381 scopus 로고    scopus 로고
    • Phylogenetic analysis, subcellular localization, and expression patterns of RPD3/HDA1 family histone deacetylases in plants
    • Alinsug MV, Yu CW, Wu K, (2009) Phylogenetic analysis, subcellular localization, and expression patterns of RPD3/HDA1 family histone deacetylases in plants. BMC Plant Biology 9: 37.
    • (2009) BMC Plant Biology , vol.9 , pp. 37
    • Alinsug, M.V.1    Yu, C.W.2    Wu, K.3
  • 5
    • 0035793060 scopus 로고    scopus 로고
    • Blocking histone deacetylation in Arabidopsis induces pleitropic effects on plant gene regulation and development
    • Tian L, Chen ZL, (2001) Blocking histone deacetylation in Arabidopsis induces pleitropic effects on plant gene regulation and development. Proc Natl Acad Sci USA 98: 200-205.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 200-205
    • Tian, L.1    Chen, Z.L.2
  • 6
    • 0141678036 scopus 로고    scopus 로고
    • Genetic control of developmental changes induced by disruption of Arabidopsis histone deacetylase 1 (AtHD1) expression
    • Tian L, Wang JJ, Fong MP, Chen M, Cao H, et al. (2003) Genetic control of developmental changes induced by disruption of Arabidopsis histone deacetylase 1 (AtHD1) expression. Genetics 165: 399-409.
    • (2003) Genetics , vol.165 , pp. 399-409
    • Tian, L.1    Wang, J.J.2    Fong, M.P.3    Chen, M.4    Cao, H.5
  • 7
    • 13744260173 scopus 로고    scopus 로고
    • Reversible histone acetylation and deacetylation mediate genome-wide, promoter-dependent and locus- specific changes in gene expression during plant development
    • Tian L, Fong MP, Wang JJ, Wei NE, Jiang H, et al. (2005) Reversible histone acetylation and deacetylation mediate genome-wide, promoter-dependent and locus- specific changes in gene expression during plant development. Genetics 169: 337-345.
    • (2005) Genetics , vol.169 , pp. 337-345
    • Tian, L.1    Fong, M.P.2    Wang, J.J.3    Wei, N.E.4    Jiang, H.5
  • 8
    • 33845730777 scopus 로고    scopus 로고
    • Arabidopsis GCN5, HD1, and TAF1/HAF2 interact to regulate histone acetylation required for light-responsive gene expression
    • Benhamed M, Bertrand C, Servet C, Zhou DX, (2006) Arabidopsis GCN5, HD1, and TAF1/HAF2 interact to regulate histone acetylation required for light-responsive gene expression. Plant Cell 18: 2893-903.
    • (2006) Plant Cell , vol.18 , pp. 2893-2903
    • Benhamed, M.1    Bertrand, C.2    Servet, C.3    Zhou, D.X.4
  • 9
    • 33744992478 scopus 로고    scopus 로고
    • TOPLESS regulates apical embryonic fate in Arabidopsis
    • Long JA, Ohno C, Smith ZR, Meyerowitz EM, (2002) TOPLESS regulates apical embryonic fate in Arabidopsis. Science 312: 1520-1523.
    • (2002) Science , vol.312 , pp. 1520-1523
    • Long, J.A.1    Ohno, C.2    Smith, Z.R.3    Meyerowitz, E.M.4
  • 10
    • 40749154400 scopus 로고    scopus 로고
    • The Arabidopsis histone deacetylases HDA6 and HDA19 contribute to the repression of embryonic properties after germination
    • Tanaka M, Kikuchi A, Kamada H, (2008) The Arabidopsis histone deacetylases HDA6 and HDA19 contribute to the repression of embryonic properties after germination. Plant Physiol 146: 149-161.
    • (2008) Plant Physiol , vol.146 , pp. 149-161
    • Tanaka, M.1    Kikuchi, A.2    Kamada, H.3
  • 11
    • 57749119423 scopus 로고    scopus 로고
    • Arabidopsis WRKY38 and WRKY62 transcription factors interact with histone deacetylase 19 in basal defense
    • Kim KC, Lai Z, Fan B, Chen Z, (2008) Arabidopsis WRKY38 and WRKY62 transcription factors interact with histone deacetylase 19 in basal defense. Plant Cell 20: 2357-71.
    • (2008) Plant Cell , vol.20 , pp. 2357-2371
    • Kim, K.C.1    Lai, Z.2    Fan, B.3    Chen, Z.4
  • 12
    • 79956045378 scopus 로고    scopus 로고
    • HDA6 interacts with FLD and regulates flowering in Arabidopsis
    • Yu CW, Liu X, Luo M, Chen C, Lin X, et al. (2011) HDA6 interacts with FLD and regulates flowering in Arabidopsis. Plant Physiol 156: 173-184.
    • (2011) Plant Physiol , vol.156 , pp. 173-184
    • Yu, C.W.1    Liu, X.2    Luo, M.3    Chen, C.4    Lin, X.5
  • 14
    • 77954763982 scopus 로고    scopus 로고
    • Involvement of Arabidopsis histone deacetylase HDA6 in ABA and salt stress response
    • Chen LT, Luo M, Wang YY, Wu K, (2010) Involvement of Arabidopsis histone deacetylase HDA6 in ABA and salt stress response. J Exp Bot 61: 3345-3353.
    • (2010) J Exp Bot , vol.61 , pp. 3345-3353
    • Chen, L.T.1    Luo, M.2    Wang, Y.Y.3    Wu, K.4
  • 15
    • 41649120400 scopus 로고    scopus 로고
    • HDA6 is required for jasmonate response, senescence and flowering in Arabidopsis
    • Wu K, Zhang L, Zhou C, Yu CW, Chaikam V, (2008) HDA6 is required for jasmonate response, senescence and flowering in Arabidopsis. J Exp Bot 59: 225-34.
    • (2008) J Exp Bot , vol.59 , pp. 225-234
    • Wu, K.1    Zhang, L.2    Zhou, C.3    Yu, C.W.4    Chaikam, V.5
  • 16
    • 33646542012 scopus 로고    scopus 로고
    • Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale gene silencing in nucleolar dominance
    • Earley K, Lawrence RJ, Pontes O, Reuther R, Enciso AJ, et al. (2006) Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale gene silencing in nucleolar dominance. Genes Dev 20: 1283-1293.
    • (2006) Genes Dev , vol.20 , pp. 1283-1293
    • Earley, K.1    Lawrence, R.J.2    Pontes, O.3    Reuther, R.4    Enciso, A.J.5
  • 17
    • 78449274516 scopus 로고    scopus 로고
    • Role of histone deacetylases HDA6 and HDA19 in ABA and abiotic stress response
    • Chen LT, Wu K, (2010) Role of histone deacetylases HDA6 and HDA19 in ABA and abiotic stress response. Plant Signal Behav 5: 1318-1320.
    • (2010) Plant Signal Behav , vol.5 , pp. 1318-1320
    • Chen, L.T.1    Wu, K.2
  • 18
    • 23944456969 scopus 로고    scopus 로고
    • HISTONE DEACETYLASE19 is involved in jasmonic acid and ethylene signaling of pathogen response in Arabidopsis
    • Zhou C, Zhang L, Duan J, Miki B, Wu K, (2005) HISTONE DEACETYLASE19 is involved in jasmonic acid and ethylene signaling of pathogen response in Arabidopsis. Plant Cell 17: 1196-204.
    • (2005) Plant Cell , vol.17 , pp. 1196-1204
    • Zhou, C.1    Zhang, L.2    Duan, J.3    Miki, B.4    Wu, K.5
  • 19
    • 26444535243 scopus 로고    scopus 로고
    • Histone acetylation affects expression of cellular patterning genes in the Arabidopsis root epidermis
    • Xu CR, Liu C, Wang YL, Li LC, Chen WQ, et al. (2005) Histone acetylation affects expression of cellular patterning genes in the Arabidopsis root epidermis. Proc Natl Acad Sci USA 102: 14469-14474.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14469-14474
    • Xu, C.R.1    Liu, C.2    Wang, Y.L.3    Li, L.C.4    Chen, W.Q.5
  • 20
    • 79953689290 scopus 로고    scopus 로고
    • Proteins of diverse function and subcellular localization are lysine acetylated in Arabidopsis
    • Finkemeier I, Laxa M, Miguet L, Howden AJM, Sweetlove LJ, (2011) Proteins of diverse function and subcellular localization are lysine acetylated in Arabidopsis. Plant Physiol 155: 1779-1790.
    • (2011) Plant Physiol , vol.155 , pp. 1779-1790
    • Finkemeier, I.1    Laxa, M.2    Miguet, L.3    Howden, A.J.M.4    Sweetlove, L.J.5
  • 21
    • 79953702814 scopus 로고    scopus 로고
    • Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis
    • Wu X, Oh MH, Schwarz EM, Larue CT, Sivaguru M, et al. (2011) Lysine acetylation is a widespread protein modification for diverse proteins in Arabidopsis. Plant Physiol 155: 1769-1778.
    • (2011) Plant Physiol , vol.155 , pp. 1769-1778
    • Wu, X.1    Oh, M.H.2    Schwarz, E.M.3    Larue, C.T.4    Sivaguru, M.5
  • 22
    • 67649381630 scopus 로고    scopus 로고
    • Subcellular localization of rice histone deacetylases in organelles
    • Chung PJ, Kim YS, Park SH, Nam BH, Kim JK, (2009) Subcellular localization of rice histone deacetylases in organelles. FEBS Letters 583: 2249-254.
    • (2009) FEBS Letters , vol.583 , pp. 2249-2254
    • Chung, P.J.1    Kim, Y.S.2    Park, S.H.3    Nam, B.H.4    Kim, J.K.5
  • 23
    • 16244366803 scopus 로고    scopus 로고
    • Class II histone deacetylases: from sequence to function, regulation, and clinical implication
    • Yang XJ, Gregoire S, (2005) Class II histone deacetylases: from sequence to function, regulation, and clinical implication. Mol Cell Biol 25: 2873-2884.
    • (2005) Mol Cell Biol , vol.25 , pp. 2873-2884
    • Yang, X.J.1    Gregoire, S.2
  • 24
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: versatile regulators
    • Verdin E, Dequiedt F, Kasler HG, (2003) Class II histone deacetylases: versatile regulators. Trends Genet 19: 286-293.
    • (2003) Trends Genet , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 26
    • 0034898560 scopus 로고    scopus 로고
    • Histone deacetylase 4 possesses intrinsic nuclear import and export signals
    • Wang AH, Yang X, (2001) Histone deacetylase 4 possesses intrinsic nuclear import and export signals. Mol Cell Biol 21: 5992-6005.
    • (2001) Mol Cell Biol , vol.21 , pp. 5992-6005
    • Wang, A.H.1    Yang, X.2
  • 27
    • 10944224581 scopus 로고    scopus 로고
    • Cytoplasmic sequestration of HDAC7 from mitochondrial and nuclear compartments upon initation of apoptosis
    • Bakin RE, Jung MO, (2004) Cytoplasmic sequestration of HDAC7 from mitochondrial and nuclear compartments upon initation of apoptosis. J Biol Chem 279: 51218-51225.
    • (2004) J Biol Chem , vol.279 , pp. 51218-51225
    • Bakin, R.E.1    Jung, M.O.2
  • 28
    • 14844344773 scopus 로고    scopus 로고
    • Association with Class IIa histone deacetylases upregulates sumoylation of MEF2 transcription factors
    • Gregoire S, Yang XJ, (2005) Association with Class IIa histone deacetylases upregulates sumoylation of MEF2 transcription factors. Mol Cell Biol 25: 2273-2287.
    • (2005) Mol Cell Biol , vol.25 , pp. 2273-2287
    • Gregoire, S.1    Yang, X.J.2
  • 29
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • Hubbert C, Guardiola A, Shao R, (2002) HDAC6 is a microtubule-associated deacetylase. Nature 417: 455-458.
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1    Guardiola, A.2    Shao, R.3
  • 30
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • Matsuyama A, Shimazu T, Sumida Y, (2002) In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation. EMBO J 21: 6820-6831.
    • (2002) EMBO J , vol.21 , pp. 6820-6831
    • Matsuyama, A.1    Shimazu, T.2    Sumida, Y.3
  • 31
    • 0037416151 scopus 로고    scopus 로고
    • HDAC6 interacts with and deacetylates tubulin and microtubules in vivo
    • Zhang Y, Li N, Caron C, (2003) HDAC6 interacts with and deacetylates tubulin and microtubules in vivo. EMBO J 22: 1168-1179.
    • (2003) EMBO J , vol.22 , pp. 1168-1179
    • Zhang, Y.1    Li, N.2    Caron, C.3
  • 32
    • 34447315270 scopus 로고    scopus 로고
    • HDAC6 modulates cell motility by altering the acetylation level of cortactin
    • Zhang X, Yuan Z, Zhang Y, (2007) HDAC6 modulates cell motility by altering the acetylation level of cortactin. Mol Cell 27: 197-213.
    • (2007) Mol Cell , vol.27 , pp. 197-213
    • Zhang, X.1    Yuan, Z.2    Zhang, Y.3
  • 33
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors
    • Bali P, Pranpat M, Bradner J, (2005) Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors. J of Biol Chem 280: 26729-26734.
    • (2005) J of Biol Chem , vol.280 , pp. 26729-26734
    • Bali, P.1    Pranpat, M.2    Bradner, J.3
  • 34
    • 27744479712 scopus 로고    scopus 로고
    • Modulating molecular chaperone Hsp90 functions through reversible acetylation
    • Aoyagi S, Archer TK, (2005) Modulating molecular chaperone Hsp90 functions through reversible acetylation. Trends Cell Biol 15: 565-567.
    • (2005) Trends Cell Biol , vol.15 , pp. 565-567
    • Aoyagi, S.1    Archer, T.K.2
  • 35
    • 33846014703 scopus 로고    scopus 로고
    • An acetylation site in the middle domain of Hsp90 regulates chaperone function
    • Scroggins BT, Robzyk K, Wang D, (2007) An acetylation site in the middle domain of Hsp90 regulates chaperone function. Mol Cell 25: 151-159.
    • (2007) Mol Cell , vol.25 , pp. 151-159
    • Scroggins, B.T.1    Robzyk, K.2    Wang, D.3
  • 36
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • Kovacs JJ, Murphy PJM, Gailliard S, (2005) HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Molecular Cell 18: 601-607.
    • (2005) Molecular Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1    Murphy, P.J.M.2    Gailliard, S.3
  • 37
    • 45149089913 scopus 로고    scopus 로고
    • HDAC6 is required for epidermal growth factor-induced B-catenin nuclear localization
    • Li Y, Zhang H, Polakiewicz RD, Yao TP, Comb MJ, (2008) HDAC6 is required for epidermal growth factor-induced B-catenin nuclear localization. J of Biol Chem 283: 12686-12690.
    • (2008) J of Biol Chem , vol.283 , pp. 12686-12690
    • Li, Y.1    Zhang, H.2    Polakiewicz, R.D.3    Yao, T.P.4    Comb, M.J.5
  • 38
    • 47749156827 scopus 로고    scopus 로고
    • HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
    • Parmigiani RB, Xu WS, Venta-Perez G, (2008) HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation. Proc Natl Acad Sci USA 105: 9633-9638.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9633-9638
    • Parmigiani, R.B.1    Xu, W.S.2    Venta-Perez, G.3
  • 39
    • 0034687741 scopus 로고    scopus 로고
    • Activation of myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase- stimulated binding of 14-3-3 to histone deacetylase 5
    • McKinsey TA, Zhang CL, Olsen EN, (2000) Activation of myocyte enhancer factor-2 transcription factor by calcium/calmodulin-dependent protein kinase- stimulated binding of 14-3-3 to histone deacetylase 5. Proc Natl Acad Sci USA 97: 14400-14405.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14400-14405
    • McKinsey, T.A.1    Zhang, C.L.2    Olsen, E.N.3
  • 40
    • 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: 760-765.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 760-765
    • Oecking, C.1    Jaspert, N.2
  • 42
    • 0036277421 scopus 로고    scopus 로고
    • Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity
    • Sehnke PC, DeLille JM, Ferl RJ, (2002) Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity. Plant Cell 14: 339-354.
    • (2002) Plant Cell , vol.14 , pp. 339-354
    • Sehnke, P.C.1    DeLille, J.M.2    Ferl, R.J.3
  • 43
    • 0037662761 scopus 로고    scopus 로고
    • 14-3-3 proteins find new partners in plant cell signaling
    • Roberts MR, (2003) 14-3-3 proteins find new partners in plant cell signaling. Trends Plant Sci 8: 218-223.
    • (2003) Trends Plant Sci , vol.8 , pp. 218-223
    • Roberts, M.R.1
  • 44
    • 1642450651 scopus 로고    scopus 로고
    • 14-3-3 proteins: regulation of signal-induced events
    • Ferl RJ, (2004) 14-3-3 proteins: regulation of signal-induced events. Physiol Plant 120: 173-178.
    • (2004) Physiol Plant , vol.120 , pp. 173-178
    • Ferl, R.J.1
  • 45
    • 65249165427 scopus 로고    scopus 로고
    • Comparative interactomics: analysis of Arabidopsis 14-3-3 complexes reveals highly conserved 14- 3-3 interactions between humans and plants
    • Paul AL, Liu L, McClung S, Laughner B, Chen S, et al. (2009) Comparative interactomics: analysis of Arabidopsis 14-3-3 complexes reveals highly conserved 14- 3-3 interactions between humans and plants. J Proteome Res 8: 1913-24.
    • (2009) J Proteome Res , vol.8 , pp. 1913-1924
    • Paul, A.L.1    Liu, L.2    McClung, S.3    Laughner, B.4    Chen, S.5
  • 46
    • 67649235671 scopus 로고    scopus 로고
    • Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana
    • Chang IF, Curran A, Woolsey R, Quilici D, Cushman JC, et al. (2009) Proteomic profiling of tandem affinity purified 14-3-3 protein complexes in Arabidopsis thaliana. Proteomics 9: 2967-2985.
    • (2009) Proteomics , vol.9 , pp. 2967-2985
    • Chang, I.F.1    Curran, A.2    Woolsey, R.3    Quilici, D.4    Cushman, J.C.5
  • 47
    • 0036914587 scopus 로고    scopus 로고
    • Metabolic enzymes as targets for 14- 3-3 proteins
    • Huber SC, MacKintosh C, Kaiser WM, (2002) Metabolic enzymes as targets for 14- 3-3 proteins. Plant Mol Biol 50: 1053-1063.
    • (2002) Plant Mol Biol , vol.50 , pp. 1053-1063
    • Huber, S.C.1    MacKintosh, C.2    Kaiser, W.M.3
  • 49
    • 0035206122 scopus 로고    scopus 로고
    • 14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG
    • Igarashi D, Ishida S, Fukazawa J, Takahashi Y, (2001) 14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG. Plant Cell 13: 2483-2497.
    • (2001) Plant Cell , vol.13 , pp. 2483-2497
    • Igarashi, D.1    Ishida, S.2    Fukazawa, J.3    Takahashi, Y.4
  • 50
    • 11944253861 scopus 로고    scopus 로고
    • Involvement of 14-3- 3 signaling protein binding in the functional regulation of the transcriptional activator REPRESSION OF SHOOT GROWTH by gibberellins
    • Ishida S, Fukazawa J, Yuasa T, Takahashi Y, (2004) Involvement of 14-3- 3 signaling protein binding in the functional regulation of the transcriptional activator REPRESSION OF SHOOT GROWTH by gibberellins. Plant Cell 16: 2641-2651.
    • (2004) Plant Cell , vol.16 , pp. 2641-2651
    • Ishida, S.1    Fukazawa, J.2    Yuasa, T.3    Takahashi, Y.4
  • 51
    • 33846037859 scopus 로고    scopus 로고
    • 14-3-3 adaptor proteins are intermediates in ABA signal transduction during barley seed germination
    • Schoonheim PJ, Sinnige MP, Casaretto JA, Veiga H, Bunney TD, et al. (2007) 14-3-3 adaptor proteins are intermediates in ABA signal transduction during barley seed germination. Plant J 49: 289-301.
    • (2007) Plant J , vol.49 , pp. 289-301
    • Schoonheim, P.J.1    Sinnige, M.P.2    Casaretto, J.A.3    Veiga, H.4    Bunney, T.D.5
  • 52
    • 0036846024 scopus 로고    scopus 로고
    • ABI5 acts downstream of ABI3 to execute an ABA-dependent growth arrest during germination
    • Lopez-Molina L, Mongrand S, McLachlin DT, Chait BT, Chua NH, (2002) ABI5 acts downstream of ABI3 to execute an ABA-dependent growth arrest during germination. Plant J 32: 317-328.
    • (2002) Plant J , vol.32 , pp. 317-328
    • Lopez-Molina, L.1    Mongrand, S.2    McLachlin, D.T.3    Chait, B.T.4    Chua, N.H.5
  • 53
    • 34547395050 scopus 로고    scopus 로고
    • An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis
    • Gampala SS, Kim TW, He JX, Tang W, Deng Z, et al. (2007) An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis. Dev Cell 13: 177-189.
    • (2007) Dev Cell , vol.13 , pp. 177-189
    • Gampala, S.S.1    Kim, T.W.2    He, J.X.3    Tang, W.4    Deng, Z.5
  • 54
    • 35748933556 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling
    • Ryu H, Kim K, Cho H, Park J, Choe S, et al. (2007) Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling. Plant Cell 19: 2749-2762.
    • (2007) Plant Cell , vol.19 , pp. 2749-2762
    • Ryu, H.1    Kim, K.2    Cho, H.3    Park, J.4    Choe, S.5
  • 56
    • 0037016696 scopus 로고    scopus 로고
    • Isolation and characterization of mammalian HDAC10, a novel histone deacetylase
    • Kao HY, Lee CH, Komarov A, Han CC, Evans RM, (2002) Isolation and characterization of mammalian HDAC10, a novel histone deacetylase. J Biol Chem 277: 187-193.
    • (2002) J Biol Chem , vol.277 , pp. 187-193
    • Kao, H.Y.1    Lee, C.H.2    Komarov, A.3    Han, C.C.4    Evans, R.M.5
  • 57
    • 0035163063 scopus 로고    scopus 로고
    • Identification of the components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways
    • Seigneurin-Berny D, Verdin A, Curtet S, Lemercier C, Garin J, et al. (2001) Identification of the components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. Mol Cell Biol 21: 8035-8044.
    • (2001) Mol Cell Biol , vol.21 , pp. 8035-8044
    • Seigneurin-Berny, D.1    Verdin, A.2    Curtet, S.3    Lemercier, C.4    Garin, J.5
  • 58
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1
    • Grozinger CM, Hassig CA, Shreiber SL, (1999) Three proteins define a class of human histone deacetylases related to yeast Hda1. Proc Natl Acad Sci USA 96: 4868-4873.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Shreiber, S.L.3
  • 59
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola AR, Yao TP, (2002) Molecular cloning and characterization of a novel histone deacetylase HDAC10. J Biol Chem 277: 3350-3356.
    • (2002) J Biol Chem , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 60
    • 0141594939 scopus 로고    scopus 로고
    • The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen- activated protein kinase signaling cascades
    • Yamamoto K, Hamada H, Shinkai H, Kohno Y, Koseki H, et al. (2003) The KDEL receptor modulates the endoplasmic reticulum stress response through mitogen- activated protein kinase signaling cascades. J Biol Chem 278: 34525-34532.
    • (2003) J Biol Chem , vol.278 , pp. 34525-34532
    • Yamamoto, K.1    Hamada, H.2    Shinkai, H.3    Kohno, Y.4    Koseki, H.5
  • 61
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • McKinsey TA, Zhang CL, Lu J, Olson EN, (2000) Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature 408: 106-111.
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1    Zhang, C.L.2    Lu, J.3    Olson, E.N.4
  • 62
    • 59049092157 scopus 로고    scopus 로고
    • Two Endoplasmic Reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels
    • Mi HK, Puglielli L, (2009) Two Endoplasmic Reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels. J Biol Chem 284: 2482-2492.
    • (2009) J Biol Chem , vol.284 , pp. 2482-2492
    • Mi, H.K.1    Puglielli, L.2
  • 63
    • 1842578986 scopus 로고    scopus 로고
    • Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
    • Gregoretti IV, Lee YM, Goodson HV, (2004) Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol 338: 17-31.
    • (2004) J Mol Biol , vol.338 , pp. 17-31
    • Gregoretti, I.V.1    Lee, Y.M.2    Goodson, H.V.3
  • 64
    • 0142135022 scopus 로고    scopus 로고
    • Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca2+/calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival
    • Linseman DA, Bartley CM, Le SS, Laessig TA, Bouchard RJ, et al. (2003) Inactivation of the myocyte enhancer factor-2 repressor histone deacetylase-5 by endogenous Ca2+/calmodulin-dependent kinase II promotes depolarization-mediated cerebellar granule neuron survival. J Biol Chem 278: 41472-41481.
    • (2003) J Biol Chem , vol.278 , pp. 41472-41481
    • Linseman, D.A.1    Bartley, C.M.2    Le, S.S.3    Laessig, T.A.4    Bouchard, R.J.5
  • 65
    • 33846534356 scopus 로고    scopus 로고
    • KIN-29 SIK regulates chemoreceptor gene expression via an MEF2 transcription factor and a Class II HDAC
    • van der Linden AM, Nolan KM, Sengupta P, (2007) KIN-29 SIK regulates chemoreceptor gene expression via an MEF2 transcription factor and a Class II HDAC. EMBO J 26: 358-370.
    • (2007) EMBO J , vol.26 , pp. 358-370
    • van der Linden, A.M.1    Nolan, K.M.2    Sengupta, P.3
  • 66
    • 34249664888 scopus 로고    scopus 로고
    • SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes
    • Berdeaux R, Goebel N, Banaszynski L, Takemori H, Wandless T, et al. (2007) SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes. Nat Med 13: 597-603.
    • (2007) Nat Med , vol.13 , pp. 597-603
    • Berdeaux, R.1    Goebel, N.2    Banaszynski, L.3    Takemori, H.4    Wandless, T.5
  • 67
    • 4544315655 scopus 로고    scopus 로고
    • Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5
    • Vega RB, Harrison BC, Meadows E, Roberts CR, Papst PJ, et al. (2004) Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5. Mol Cell Biol 24: 8374-8385.
    • (2004) Mol Cell Biol , vol.24 , pp. 8374-8385
    • Vega, R.B.1    Harrison, B.C.2    Meadows, E.3    Roberts, C.R.4    Papst, P.J.5
  • 68
    • 17144414861 scopus 로고    scopus 로고
    • Protein kinase D1 phosphorylates HDAC7 and Induces its nuclear export after TCR activation
    • Parra M, Kasler H, McKinsey TA, Olson EN, Verdin E, (2005) Protein kinase D1 phosphorylates HDAC7 and Induces its nuclear export after TCR activation. J Biol Chem 280: 13762-13770.
    • (2005) J Biol Chem , vol.280 , pp. 13762-13770
    • Parra, M.1    Kasler, H.2    McKinsey, T.A.3    Olson, E.N.4    Verdin, E.5
  • 69
    • 15444375044 scopus 로고    scopus 로고
    • Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor- induced Nur77 expression and apoptosis
    • Dequiedt F, Van Lint J, Lecomte E, Van Duppen V, Seufferlein T, et al. (2005) Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor- induced Nur77 expression and apoptosis. J Exp Med 201: 793-804.
    • (2005) J Exp Med , vol.201 , pp. 793-804
    • Dequiedt, F.1    van Lint, J.2    Lecomte, E.3    van Duppen, V.4    Seufferlein, T.5
  • 70
    • 34547919621 scopus 로고    scopus 로고
    • Class IIa histone deacetylases: regulating the regulators
    • Martin M, Kettmann R, Dequiedt F, (2007) Class IIa histone deacetylases: regulating the regulators. Oncogene 26: 5450-5467.
    • (2007) Oncogene , vol.26 , pp. 5450-5467
    • Martin, M.1    Kettmann, R.2    Dequiedt, F.3
  • 71
    • 20444420893 scopus 로고    scopus 로고
    • An expression screen reveals modulators of class II histone deacetylase phosphorylation
    • Chang S, Bezprozvannaya S, Li S, Olson EN, (2005) An expression screen reveals modulators of class II histone deacetylase phosphorylation. Proc Natl Acad Sci USA 102: 8120-8125.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8120-8125
    • Chang, S.1    Bezprozvannaya, S.2    Li, S.3    Olson, E.N.4
  • 72
    • 34247640762 scopus 로고    scopus 로고
    • Identification of novel substrates for human checkpoint kinase Chk1 and Chk2 through genome-wide screening using a consensus Chk phosphorylation motif
    • Kim MA, Kim HJ, Brown AL, Lee MY, Bae YS, et al. (2007) Identification of novel substrates for human checkpoint kinase Chk1 and Chk2 through genome-wide screening using a consensus Chk phosphorylation motif. Exp Mol Med 39: 205-212.
    • (2007) Exp Mol Med , vol.39 , pp. 205-212
    • Kim, M.A.1    Kim, H.J.2    Brown, A.L.3    Lee, M.Y.4    Bae, Y.S.5
  • 73
    • 3943054839 scopus 로고    scopus 로고
    • The Sirt2 family of protein deacetylases
    • Blander G, Guarente L, (2004) The Sirt2 family of protein deacetylases. Annu Rev Biochem 73: 417-435.
    • (2004) Annu Rev Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 74
    • 0037135972 scopus 로고    scopus 로고
    • The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase
    • Schwer B, North BJ, Frye RA, Ott M, Verdin E, (2002) The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. J Cell Biol 158: 647-657.
    • (2002) J Cell Biol , vol.158 , pp. 647-657
    • Schwer, B.1    North, B.J.2    Frye, R.A.3    Ott, M.4    Verdin, E.5
  • 75
    • 77955891911 scopus 로고    scopus 로고
    • The epigenome and the mitochondrion: bioenergetics and the environment
    • Wallace DC, (2010) The epigenome and the mitochondrion: bioenergetics and the environment. Genes Dev 24: 1571-1573.
    • (2010) Genes Dev , vol.24 , pp. 1571-1573
    • Wallace, D.C.1
  • 76
    • 70450231612 scopus 로고    scopus 로고
    • Energetics, epigenetics, mitochondrial genetics
    • Wallace DC, Fan W, (2010) Energetics, epigenetics, mitochondrial genetics. Mitochondrion 10: 12-31.
    • (2010) Mitochondrion , vol.10 , pp. 12-31
    • Wallace, D.C.1    Fan, W.2
  • 77
    • 0038795543 scopus 로고    scopus 로고
    • The transcriptional enhancer of the pea plastocyanin gene associates with the nuclear matrix and regulates gene expression through histone acetylation
    • Chua YL, Watson LA, Gray JC, (2003) The transcriptional enhancer of the pea plastocyanin gene associates with the nuclear matrix and regulates gene expression through histone acetylation. Plant Cell 15: 1468-1479.
    • (2003) Plant Cell , vol.15 , pp. 1468-1479
    • Chua, Y.L.1    Watson, L.A.2    Gray, J.C.3
  • 78
    • 33644745113 scopus 로고    scopus 로고
    • Quantitative effects of vernalization on FLC and SOC1 expression
    • Sheldon CC, Finnegan EJ, Dennis ES, Peacock WJ, (2006) Quantitative effects of vernalization on FLC and SOC1 expression. Plant J 45: 871-883.
    • (2006) Plant J , vol.45 , pp. 871-883
    • Sheldon, C.C.1    Finnegan, E.J.2    Dennis, E.S.3    Peacock, W.J.4
  • 79
    • 34249787308 scopus 로고    scopus 로고
    • Roles of dynamic and reversible histone acetylation in plant development and polyploidy
    • Chen ZJ, Tian L, (2007) Roles of dynamic and reversible histone acetylation in plant development and polyploidy. Biochim Biophys Acta 1769: 295-307.
    • (2007) Biochim Biophys Acta , vol.1769 , pp. 295-307
    • Chen, Z.J.1    Tian, L.2
  • 80
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium- mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF, (1998) Floral dip: A simplified method for Agrobacterium- mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 81
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP:cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency
    • Cutler S, Ehrhardt DW, Griffitts JS, Somerville CR, (2000) Random GFP:cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at high frequency. Proc Natl Acad Sci USA 97: 3718-3723.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3718-3723
    • Cutler, S.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 82
    • 34447099171 scopus 로고    scopus 로고
    • Arabidopsis mesophyll protoplasts: a versatile cell system for transient gene expression analysis
    • Yoo SD, Cho YH, Sheen J, (2007) Arabidopsis mesophyll protoplasts: a versatile cell system for transient gene expression analysis. Nat Protoc 2: 1565-1572.
    • (2007) Nat Protoc , vol.2 , pp. 1565-1572
    • Yoo, S.D.1    Cho, Y.H.2    Sheen, J.3
  • 83
    • 38449110969 scopus 로고    scopus 로고
    • Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells
    • Miao Y, Jiang L, (2007) Transient expression of fluorescent fusion proteins in protoplasts of suspension cultured cells. Nat Protocols 2: 2348-2352.
    • (2007) Nat Protocols , vol.2 , pp. 2348-2352
    • Miao, Y.1    Jiang, L.2
  • 84
    • 54849417596 scopus 로고    scopus 로고
    • Vectors for multi-color bimolecular fluorescence complementation to investigate protein-protein interactions in living plant cells
    • Lee LY, Fang MJ, Kuang LY, Gelvin SB, (2008) Vectors for multi-color bimolecular fluorescence complementation to investigate protein-protein interactions in living plant cells. Plant Methods 4: 24.
    • (2008) Plant Methods , vol.4 , pp. 24
    • Lee, L.Y.1    Fang, M.J.2    Kuang, L.Y.3    Gelvin, S.B.4
  • 85
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • Nelson BK, Cai X, Nebenfuhr A, (2007) A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J 51: 1126-1136.
    • (2007) Plant J , vol.51 , pp. 1126-1136
    • Nelson, B.K.1    Cai, X.2    Nebenfuhr, A.3
  • 86
    • 35748933556 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling
    • Ryu H, Kim K, Cho H, Park J, Choe S, et al. (2007) Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling. Plant Cell 19: 2749-2762.
    • (2007) Plant Cell , vol.19 , pp. 2749-2762
    • Ryu, H.1    Kim, K.2    Cho, H.3    Park, J.4    Choe, S.5
  • 87
    • 0141963860 scopus 로고    scopus 로고
    • Differential regulation of EIN3 stability by glucose and ethylene signaling in plants
    • Yanagisawa S, Yoo SD, Sheen J, (2003) Differential regulation of EIN3 stability by glucose and ethylene signaling in plants. Nature 425: 521-525.
    • (2003) Nature , vol.425 , pp. 521-525
    • Yanagisawa, S.1    Yoo, S.D.2    Sheen, J.3
  • 88
    • 0038028737 scopus 로고    scopus 로고
    • Rha1, an Arabidopsis Rab5 homolog, plays a critical role in the vacuolar trafficking of soluble cargo proteins
    • Sohn EJ, Kim ES, Zhao M, Kim SJ, Kim H, et al. (2003) Rha1, an Arabidopsis Rab5 homolog, plays a critical role in the vacuolar trafficking of soluble cargo proteins. Plant Cell 15: 1057-1070.
    • (2003) Plant Cell , vol.15 , pp. 1057-1070
    • Sohn, E.J.1    Kim, E.S.2    Zhao, M.3    Kim, S.J.4    Kim, H.5
  • 89
    • 73849110791 scopus 로고    scopus 로고
    • Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components and anchoring nucleoporin
    • Lu Q, Tang X, Tian G, Wang F, Liu K, et al. (2010) Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components and anchoring nucleoporin. Plant J 61: 259-270.
    • (2010) Plant J , vol.61 , pp. 259-270
    • Lu, Q.1    Tang, X.2    Tian, G.3    Wang, F.4    Liu, K.5


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