메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages

Regulation of the Regulators: Post-Translational Modifications, Subcellular, and Spatiotemporal Distribution of Plant 14-3-3 Proteins

Author keywords

14 3 3; phosphorylation; plants; post translational modifications; subcellular localization

Indexed keywords


EID: 85015421447     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2016.00611     Document Type: Review
Times cited : (56)

References (70)
  • 1
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • Agrawal G. K. Thelen J. J. (2006). Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol. Cell. Proteomics 5, 2044–2059. 10.1074/mcp.M600084-MCP200
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2044-2059
    • Agrawal, G.K.1    Thelen, J.J.2
  • 3
    • 0027333424 scopus 로고
    • Signal transduction in guard cells
    • 8280465
    • Assmann S. M. (1993). Signal transduction in guard cells. Annu. Rev. Cell Biol. 9, 345–375. 10.1146/annurev.cb.09.110193.0020218280465
    • (1993) Annu. Rev. Cell Biol , vol.9 , pp. 345-375
    • Assmann, S.M.1
  • 4
    • 0029924885 scopus 로고    scopus 로고
    • The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein
    • 8674533
    • Bachmann M. Huber J. L. Liao P. C. Gage D. A. Huber S. C. (1996). The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein. FEBS Lett. 387, 127–131. 10.1016/0014-5793(96)00478-48674533
    • (1996) FEBS Lett , vol.387 , pp. 127-131
    • Bachmann, M.1    Huber, J.L.2    Liao, P.C.3    Gage, D.A.4    Huber, S.C.5
  • 6
    • 33644792657 scopus 로고    scopus 로고
    • TPK1 is a vacuolar ion channel different from the slow-vacuolar cation channel
    • 16113216
    • Bihler H. Eing C. Hebeisen S. Roller A. Czempinski K. Bertl A. (2005). TPK1 is a vacuolar ion channel different from the slow-vacuolar cation channel. Plant Physiol. 139, 417–424. 10.1104/pp.105.06559916113216
    • (2005) Plant Physiol , vol.139 , pp. 417-424
    • Bihler, H.1    Eing, C.2    Hebeisen, S.3    Roller, A.4    Czempinski, K.5    Bertl, A.6
  • 7
    • 43549121485 scopus 로고    scopus 로고
    • Transcription profiling of soybean nodulation by Bradyrhizobium japonicum
    • 18393623
    • Brechenmacher L. Kim M. Y. Benitez M. Li M. Joshi T. Calla B. et al. (2008). Transcription profiling of soybean nodulation by Bradyrhizobium japonicum. Mol. Plant Microb. Interact. 21, 631–645. 10.1094/MPMI-21-5-063118393623
    • (2008) Mol. Plant Microb. Interact , vol.21 , pp. 631-645
    • Brechenmacher, L.1    Kim, M.Y.2    Benitez, M.3    Li, M.4    Joshi, T.5    Calla, B.6
  • 8
    • 0037018148 scopus 로고    scopus 로고
    • 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport
    • 11864996
    • Brunet A. Kanai F. Stehn J. Xu J. Sarbassova D. Frangioni J. V. et al. (2002). 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. J. Cell Biol. 156, 817–828. 10.1083/jcb.20011205911864996
    • (2002) J. Cell Biol , vol.156 , pp. 817-828
    • Brunet, A.1    Kanai, F.2    Stehn, J.3    Xu, J.4    Sarbassova, D.5    Frangioni, J.V.6
  • 9
    • 0035957331 scopus 로고    scopus 로고
    • 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase
    • 11274449
    • Bunney T. D. van Walraven H. S. de Boer A. H. (2001). 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase. Proc. Natl. Acad. Sci. U.S.A. 98, 4249–4254. 10.1073/pnas.06143749811274449
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 4249-4254
    • Bunney, T.D.1    van Walraven, H.S.2    de Boer, A.H.3
  • 10
    • 84907452203 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 protein RARE COLD INDUCIBLE 1A links low-temperature response and ethylene biosynthesis to regulate freezing tolerance and cold acclimation
    • 25122152
    • Catala R. Lopez-Cobollo R. Mar Castellano M. Angosto T. Alonso J. M. Ecker J. R. et al. (2014). The Arabidopsis 14-3-3 protein RARE COLD INDUCIBLE 1A links low-temperature response and ethylene biosynthesis to regulate freezing tolerance and cold acclimation. Plant Cell 26, 3326–3342. 10.1105/tpc.114.12760525122152
    • (2014) Plant Cell , vol.26 , pp. 3326-3342
    • Catala, R.1    Lopez-Cobollo, R.2    Mar Castellano, M.3    Angosto, T.4    Alonso, J.M.5    Ecker, J.R.6
  • 11
    • 27744523654 scopus 로고    scopus 로고
    • C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors
    • 16123035
    • Coblitz B. Shikano S. Wu M. Gabelli S. B. Cockrell L. M. Spieker M. et al. (2005). C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors. J. Biol. Chem. 280, 36263–36272. 10.1074/jbc.M50755920016123035
    • (2005) J. Biol. Chem , vol.280 , pp. 36263-36272
    • Coblitz, B.1    Shikano, S.2    Wu, M.3    Gabelli, S.B.4    Cockrell, L.M.5    Spieker, M.6
  • 12
    • 0030220501 scopus 로고    scopus 로고
    • Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene
    • 8776894
    • Daugherty C. J. Rooney M. F. Miller P. W. Ferl R. J. (1996). Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene. Plant Cell 8, 1239–1248. 10.1105/tpc.8.8.12398776894
    • (1996) Plant Cell , vol.8 , pp. 1239-1248
    • Daugherty, C.J.1    Rooney, M.F.2    Miller, P.W.3    Ferl, R.J.4
  • 13
    • 84888083373 scopus 로고    scopus 로고
    • Phosphorylation-related modification at the dimer interface of 14-3-3omega dramatically alters monomer interaction dynamics
    • 24211434
    • Denison F. C. Gokirmak T. Ferl R. J. (2014). Phosphorylation-related modification at the dimer interface of 14-3-3omega dramatically alters monomer interaction dynamics. Arch. Biochem. Biophys. 541, 1–12. 10.1016/j.abb.2013.10.02524211434
    • (2014) Arch. Biochem. Biophys , vol.541 , pp. 1-12
    • Denison, F.C.1    Gokirmak, T.2    Ferl, R.J.3
  • 14
    • 81355138163 scopus 로고    scopus 로고
    • Determining novel functions of Arabidopsis 14-3-3 proteins in central metabolic processes
    • 22104211
    • Diaz C. Kusano M. Sulpice R. Araki M. Redestig H. Saito K. et al. (2011). Determining novel functions of Arabidopsis 14-3-3 proteins in central metabolic processes. BMC Syst. Biol. 5:192. 10.1186/1752-0509-5-19222104211
    • (2011) BMC Syst. Biol , vol.5 , pp. 192
    • Diaz, C.1    Kusano, M.2    Sulpice, R.3    Araki, M.4    Redestig, H.5    Saito, K.6
  • 15
    • 84919341384 scopus 로고    scopus 로고
    • Affinity chromatography revealed insights into unique functionality of two 14-3-3 protein species in developing maize kernels
    • 25449830
    • Dou Y. Liu X. Yin Y. Han S. Lu Y. Liu Y. et al. (2015). Affinity chromatography revealed insights into unique functionality of two 14-3-3 protein species in developing maize kernels. J. Proteomics 114, 274–286. 10.1016/j.jprot.2014.10.01925449830
    • (2015) J. Proteomics , vol.114 , pp. 274-286
    • Dou, Y.1    Liu, X.2    Yin, Y.3    Han, S.4    Lu, Y.5    Liu, Y.6
  • 16
    • 0028083035 scopus 로고
    • Evolutionary implications of the family of 14-3-3 brain protein homologs in Arabidopsis thaliana
    • 7958937
    • Ferl R. J. Lu G. Bowen B. W. (1994). Evolutionary implications of the family of 14-3-3 brain protein homologs in Arabidopsis thaliana. Genetica 92, 129–138. 10.1007/BF001637627958937
    • (1994) Genetica , vol.92 , pp. 129-138
    • Ferl, R.J.1    Lu, G.2    Bowen, B.W.3
  • 17
    • 0033579441 scopus 로고    scopus 로고
    • +)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947)
    • 10593986
    • +)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947). J. Biol. Chem. 274, 36774–36780. 10.1074/jbc.274.51.3677410593986
    • (1999) J. Biol. Chem , vol.274 , pp. 36774-36780
    • Fuglsang, A.T.1    Visconti, S.2    Drumm, K.3    Jahn, T.4    Stensballe, A.5    Mattei, B.6
  • 18
    • 33744482032 scopus 로고    scopus 로고
    • Proteomic analysis of the 14-3-3 family in Arabidopsis
    • 16619310
    • Fuller B. Stevens S. M. Jr. Sehnke P. C. Ferl R. J. (2006). Proteomic analysis of the 14-3-3 family in Arabidopsis. Proteomics 6, 3050–3059. 10.1002/pmic.20050072916619310
    • (2006) Proteomics , vol.6 , pp. 3050-3059
    • Fuller, B.1    Stevens, S.M.2    Sehnke, P.C.3    Ferl, R.J.4
  • 19
    • 34547395050 scopus 로고    scopus 로고
    • An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis
    • 17681130
    • Gampala S. S. Kim T. W. He J. X. Tang W. Deng Z. Bai M. Y. et al. (2007). An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis. Dev. Cell 13, 177–189. 10.1016/j.devcel.2007.06.00917681130
    • (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    Bai, M.Y.6
  • 20
    • 84939249102 scopus 로고    scopus 로고
    • Light modulated activity of root alkaline/neutral invertase involves the interaction with 14-3-3 proteins
    • 25256212
    • Gao J. van Kleeff P. J. Oecking C. Li K. W. Erban A. Kopka J. et al. (2014). Light modulated activity of root alkaline/neutral invertase involves the interaction with 14-3-3 proteins. Plant J. 80, 785–796. 10.1111/tpj.1267725256212
    • (2014) Plant J , vol.80 , pp. 785-796
    • Gao, J.1    van Kleeff, P.J.2    Oecking, C.3    Li, K.W.4    Erban, A.5    Kopka, J.6
  • 21
    • 34548191317 scopus 로고    scopus 로고
    • Proteomic analysis of near-isogenic sunflower varieties differing in seed oil traits
    • 17580850
    • Hajduch M. Casteel J. E. Tang S. Hearne L. B. Knapp S. Thelen J. J. (2007). Proteomic analysis of near-isogenic sunflower varieties differing in seed oil traits. J. Proteome Res. 6, 3232–3241. 10.1021/pr070149a17580850
    • (2007) J. Proteome Res , vol.6 , pp. 3232-3241
    • Hajduch, M.1    Casteel, J.E.2    Tang, S.3    Hearne, L.B.4    Knapp, S.5    Thelen, J.J.6
  • 23
    • 77950524249 scopus 로고    scopus 로고
    • Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression
    • 20118269
    • Hajduch M. Hearne L. B. Miernyk J. A. Casteel J. E. Joshi T. Agrawal G. K. et al. (2010). Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression. Plant Physiol. 152, 2078–2087. 10.1104/pp.109.15241320118269
    • (2010) Plant Physiol , vol.152 , pp. 2078-2087
    • Hajduch, M.1    Hearne, L.B.2    Miernyk, J.A.3    Casteel, J.E.4    Joshi, T.5    Agrawal, G.K.6
  • 24
    • 84929660141 scopus 로고    scopus 로고
    • Involvement of 14-3-3 protein GRF9 in root growth and response under polyethylene glycol-induced water stress
    • 25873671
    • He Y. Wu J. Lv B. Li J. Gao Z. Xu W. et al. (2015). Involvement of 14-3-3 protein GRF9 in root growth and response under polyethylene glycol-induced water stress. J. Exp. Bot. 66, 2271–2281. 10.1093/jxb/erv14925873671
    • (2015) J. Exp. Bot , vol.66 , pp. 2271-2281
    • He, Y.1    Wu, J.2    Lv, B.3    Li, J.4    Gao, Z.5    Xu, W.6
  • 25
    • 70349644993 scopus 로고    scopus 로고
    • Quantitative proteomics of seed filling in castor: comparison with soybean and rapeseed reveals differences between photosynthetic and nonphotosynthetic seed metabolism
    • 19675154
    • Houston N. L. Hajduch M. Thelen J. J. (2009). Quantitative proteomics of seed filling in castor: comparison with soybean and rapeseed reveals differences between photosynthetic and nonphotosynthetic seed metabolism. Plant Physiol. 151, 857–868. 10.1104/pp.109.14162219675154
    • (2009) Plant Physiol , vol.151 , pp. 857-868
    • Houston, N.L.1    Hajduch, M.2    Thelen, J.J.3
  • 26
    • 0000621511 scopus 로고
    • Comparative studies of the light modulation of nitrate reductase and sucrose-phosphate synthase activities in spinach leaves
    • 16653049
    • Huber S. C. Huber J. L. Campbell W. H. Redinbaugh M. G. (1992). Comparative studies of the light modulation of nitrate reductase and sucrose-phosphate synthase activities in spinach leaves. Plant Physiol. 100, 706–712. 10.1104/pp.100.2.70616653049
    • (1992) Plant Physiol , vol.100 , pp. 706-712
    • Huber, S.C.1    Huber, J.L.2    Campbell, W.H.3    Redinbaugh, M.G.4
  • 27
    • 0035206122 scopus 로고    scopus 로고
    • 14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG
    • 11701883
    • 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. 10.1105/tpc.13.11.248311701883
    • (2001) Plant Cell , vol.13 , pp. 2483-2497
    • Igarashi, D.1    Ishida, S.2    Fukazawa, J.3    Takahashi, Y.4
  • 28
    • 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
    • 15377759
    • 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. 10.1105/tpc.104.02460415377759
    • (2004) Plant Cell , vol.16 , pp. 2641-2651
    • Ishida, S.1    Fukazawa, J.2    Yuasa, T.3    Takahashi, Y.4
  • 29
    • 33845386374 scopus 로고    scopus 로고
    • Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix
    • 17137349
    • Ito J. Heazlewood J. L. Millar A. H. (2006). Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix. J. Proteome Res. 5, 3459–3469. 10.1021/pr060403j17137349
    • (2006) J. Proteome Res , vol.5 , pp. 3459-3469
    • Ito, J.1    Heazlewood, J.L.2    Millar, A.H.3
  • 31
    • 63349091729 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana
    • 19245862
    • Jones A. M. MacLean D. Studholme D. J. Serna-Sanz A. Andreasson E. Rathjen J. P. et al. (2009). Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana. J. Proteomics 72, 439–451. 10.1016/j.jprot.2009.02.00419245862
    • (2009) J. Proteomics , vol.72 , pp. 439-451
    • Jones, A.M.1    MacLean, D.2    Studholme, D.J.3    Serna-Sanz, A.4    Andreasson, E.5    Rathjen, J.P.6
  • 32
    • 0033570171 scopus 로고    scopus 로고
    • +)-ATPase by phosphorylation of the C-terminus in stomatal guard cells
    • 10523299
    • +)-ATPase by phosphorylation of the C-terminus in stomatal guard cells. EMBO J. 18, 5548–5558. 10.1093/emboj/18.20.554810523299
    • (1999) EMBO J , vol.18 , pp. 5548-5558
    • Kinoshita, T.1    Shimazaki, K.2
  • 33
    • 0035020975 scopus 로고    scopus 로고
    • +-ATPase in response to fusicoccin
    • 11333314
    • +-ATPase in response to fusicoccin. Plant Cell Physiol. 42, 424–432. 10.1093/pcp/pce05511333314
    • (2001) Plant Cell Physiol , vol.42 , pp. 424-432
    • Kinoshita, T.1    Shimazaki, K.2
  • 35
    • 77956568287 scopus 로고    scopus 로고
    • Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase
    • 20690630
    • Lambeck I. Chi J. C. Krizowski S. Mueller S. Mehlmer N. Teige M. et al. (2010). Kinetic analysis of 14-3-3-inhibited Arabidopsis thaliana nitrate reductase. Biochemistry 49, 8177–8186. 10.1021/bi100348720690630
    • (2010) Biochemistry , vol.49 , pp. 8177-8186
    • Lambeck, I.1    Chi, J.C.2    Krizowski, S.3    Mueller, S.4    Mehlmer, N.5    Teige, M.6
  • 36
    • 33744958732 scopus 로고    scopus 로고
    • Regulation of Arabidopsis thaliana 14-3-3 gene expression by gamma-aminobutyric acid
    • 17080964
    • Lancien M. Roberts M. R. (2006). Regulation of Arabidopsis thaliana 14-3-3 gene expression by gamma-aminobutyric acid. Plant Cell Environ. 29, 1430–1436. 10.1111/j.1365-3040.2006.01526.x17080964
    • (2006) Plant Cell Environ , vol.29 , pp. 1430-1436
    • Lancien, M.1    Roberts, M.R.2
  • 39
    • 0033552943 scopus 로고    scopus 로고
    • Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein
    • 9923681
    • Lopez-Girona A. Furnari B. Mondesert O. Russell P. (1999). Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 397, 172–175. 10.1038/164889923681
    • (1999) Nature , vol.397 , pp. 172-175
    • Lopez-Girona, A.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 40
    • 0028675630 scopus 로고
    • The 30-kilodalton protein present in purified fusicoccin receptor preparations is a 14-3-3-like protein
    • 7846161
    • Marra M. Fullone M. R. Fogliano V. Pen J. Mattei M. Masi S. et al. (1994). The 30-kilodalton protein present in purified fusicoccin receptor preparations is a 14-3-3-like protein. Plant Physiol. 106, 1497–1501. 10.1104/pp.106.4.14977846161
    • (1994) Plant Physiol , vol.106 , pp. 1497-1501
    • Marra, M.1    Fullone, M.R.2    Fogliano, V.3    Pen, J.4    Mattei, M.5    Masi, S.6
  • 41
    • 0033950443 scopus 로고    scopus 로고
    • 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants
    • 10634907
    • May T. Soll J. (2000). 14-3-3 proteins form a guidance complex with chloroplast precursor proteins in plants. Plant Cell 12, 53–64. 10.1105/tpc.12.1.5310634907
    • (2000) Plant Cell , vol.12 , pp. 53-64
    • May, T.1    Soll, J.2
  • 42
    • 84866734200 scopus 로고    scopus 로고
    • Characterization of the phosphoproteome of mature Arabidopsis pollen
    • 22631563
    • Mayank P. Grossman J. Wuest S. Boisson-Dernier A. Roschitzki B. Nanni P. et al. (2012). Characterization of the phosphoproteome of mature Arabidopsis pollen. Plant J. 72, 89–101. 10.1111/j.1365-313X.2012.05061.x22631563
    • (2012) Plant J , vol.72 , pp. 89-101
    • Mayank, P.1    Grossman, J.2    Wuest, S.3    Boisson-Dernier, A.4    Roschitzki, B.5    Nanni, P.6
  • 43
    • 37249004253 scopus 로고    scopus 로고
    • The 14-3-3 proteins mu and upsilon influence transition to flowering and early phytochrome response
    • 17951453
    • Mayfield J. D. Folta K. M. Paul A. L. Ferl R. J. (2007). The 14-3-3 proteins mu and upsilon influence transition to flowering and early phytochrome response. Plant Physiol. 145, 1692–1702. 10.1104/pp.107.10865417951453
    • (2007) Plant Physiol , vol.145 , pp. 1692-1702
    • Mayfield, J.D.1    Folta, K.M.2    Paul, A.L.3    Ferl, R.J.4
  • 44
    • 84861398943 scopus 로고    scopus 로고
    • The 14-3-3 proteins of Arabidopsis regulate root growth and chloroplast development as components of the photosensory system
    • 22378945
    • Mayfield J. D. Paul A. L. Ferl R. J. (2012). The 14-3-3 proteins of Arabidopsis regulate root growth and chloroplast development as components of the photosensory system. J. Exp. Bot. 63, 3061–3070. 10.1093/jxb/ers02222378945
    • (2012) J. Exp. Bot , vol.63 , pp. 3061-3070
    • Mayfield, J.D.1    Paul, A.L.2    Ferl, R.J.3
  • 45
    • 77954891925 scopus 로고    scopus 로고
    • +)-dependent protein kinase CPK3 is required for MAPK-independent salt-stress acclimation in Arabidopsis
    • 20497378
    • +)-dependent protein kinase CPK3 is required for MAPK-independent salt-stress acclimation in Arabidopsis. Plant J. 63, 484–489. 10.1111/j.1365-313X.2010.04257.x20497378
    • (2010) Plant J , vol.63 , pp. 484-489
    • Mehlmer, N.1    Wurzinger, B.2    Stael, S.3    Hofmann-Rodrigues, D.4    Csaszar, E.5    Pfister, B.6
  • 46
    • 77954247252 scopus 로고    scopus 로고
    • Large-scale comparative phosphoproteomics identifies conserved phosphorylation sites in plants
    • 20466843
    • Nakagami H. Sugiyama N. Mochida K. Daudi A. Yoshida Y. Toyoda T. et al. (2010). Large-scale comparative phosphoproteomics identifies conserved phosphorylation sites in plants. Plant Physiol. 153, 1161–1174. 10.1104/pp.110.15734720466843
    • (2010) Plant Physiol , vol.153 , pp. 1161-1174
    • Nakagami, H.1    Sugiyama, N.2    Mochida, K.3    Daudi, A.4    Yoshida, Y.5    Toyoda, T.6
  • 47
    • 0027933175 scopus 로고
    • The fusicoccin receptor of plants is a member of the 14-3-3 superfamily of eukaryotic regulatory proteins
    • 7925968
    • Oecking C. Eckerskorn C. Weiler E. W. (1994). The fusicoccin receptor of plants is a member of the 14-3-3 superfamily of eukaryotic regulatory proteins. FEBS Lett. 352, 163–166. 10.1016/0014-5793(94)00949-X7925968
    • (1994) FEBS Lett , vol.352 , pp. 163-166
    • Oecking, C.1    Eckerskorn, C.2    Weiler, E.W.3
  • 48
    • 0030879911 scopus 로고    scopus 로고
    • Topology and target interaction of the fusicoccin-binding 14-3-3 homologs of Commelina communis
    • Oecking C. Piotrowski M. Hagemeier J. Hagemann K. (1997). Topology and target interaction of the fusicoccin-binding 14-3-3 homologs of Commelina communis. Plant J. 12, 441–453. 10.1046/j.1365-313X.1997.12020441.x
    • (1997) Plant J , vol.12 , pp. 441-453
    • Oecking, C.1    Piotrowski, M.2    Hagemeier, J.3    Hagemann, K.4
  • 51
    • 0033177889 scopus 로고    scopus 로고
    • Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complex
    • 10449590
    • Pan S. Sehnke P. C. Ferl R. J. Gurley W. B. (1999). Specific interactions with TBP and TFIIB in vitro suggest that 14-3-3 proteins may participate in the regulation of transcription when part of a DNA binding complex. Plant Cell 11, 1591–1602. 10.1105/tpc.11.8.159110449590
    • (1999) Plant Cell , vol.11 , pp. 1591-1602
    • Pan, S.1    Sehnke, P.C.2    Ferl, R.J.3    Gurley, W.B.4
  • 52
    • 16344373193 scopus 로고    scopus 로고
    • Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions
    • 15659648
    • Paul A. L. Sehnke P. C. Ferl R. J. (2005). Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions. Mol. Biol. Cell 16, 1735–1743. 10.1091/mbc.E04-09-083915659648
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1735-1743
    • Paul, A.L.1    Sehnke, P.C.2    Ferl, R.J.3
  • 53
    • 84870849985 scopus 로고    scopus 로고
    • 14-3-3 proteins SGF14c and SGF14l play critical roles during soybean nodulation
    • 23060368
    • Radwan O. Wu X. Govindarajulu M. Libault M. Neece D. J. Oh M. H. et al. (2012). 14-3-3 proteins SGF14c and SGF14l play critical roles during soybean nodulation. Plant Physiol. 160, 2125–2136. 10.1104/pp.112.20702723060368
    • (2012) Plant Physiol , vol.160 , pp. 2125-2136
    • Radwan, O.1    Wu, X.2    Govindarajulu, M.3    Libault, M.4    Neece, D.J.5    Oh, M.H.6
  • 54
    • 66649127498 scopus 로고    scopus 로고
    • Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks
    • 19376835
    • Reiland S. Messerli G. Baerenfaller K. Gerrits B. Endler A. Grossmann J. et al. (2009). Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks. Plant Physiol. 150, 889–903. 10.1104/pp.109.13867719376835
    • (2009) Plant Physiol , vol.150 , pp. 889-903
    • Reiland, S.1    Messerli, G.2    Baerenfaller, K.3    Gerrits, B.4    Endler, A.5    Grossmann, J.6
  • 55
    • 80053563165 scopus 로고    scopus 로고
    • Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis
    • 21668537
    • Sato T. Maekawa S. Yasuda S. Domeki Y. Sueyoshi K. Fujiwara M. et al. (2011). Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis. Plant J. 68, 137–146. 10.1111/j.1365-313X.2011.04673.x21668537
    • (2011) Plant J , vol.68 , pp. 137-146
    • Sato, T.1    Maekawa, S.2    Yasuda, S.3    Domeki, Y.4    Sueyoshi, K.5    Fujiwara, M.6
  • 56
    • 16244362244 scopus 로고    scopus 로고
    • A gene expression map of Arabidopsis thaliana development
    • 15806101
    • Schmid M. Davison T. S. Henz S. R. Pape U. J. Demar M. Vingron M. et al. (2005). A gene expression map of Arabidopsis thaliana development. Nat. Genet. 37, 501–506. 10.1038/ng154315806101
    • (2005) Nat. Genet , vol.37 , pp. 501-506
    • Schmid, M.1    Davison, T.S.2    Henz, S.R.3    Pape, U.J.4    Demar, M.5    Vingron, M.6
  • 57
    • 0035895274 scopus 로고    scopus 로고
    • Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
    • 11149942
    • Sehnke P. C. Chung H. J. Wu K. Ferl R. J. (2001). Regulation of starch accumulation by granule-associated plant 14-3-3 proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 765–770. 10.1073/pnas.98.2.76511149942
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 765-770
    • Sehnke, P.C.1    Chung, H.J.2    Wu, K.3    Ferl, R.J.4
  • 58
    • 34547509284 scopus 로고    scopus 로고
    • Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes
    • 17404219
    • Shin R. Alvarez S. Burch A. Y. Jez J. M. Schachtman D. P. (2007). Phosphoproteomic identification of targets of the Arabidopsis sucrose nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic processes. Proc. Natl. Acad. Sci. U.S.A. 104, 6460–6465. 10.1073/pnas.061020810417404219
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 6460-6465
    • Shin, R.1    Alvarez, S.2    Burch, A.Y.3    Jez, J.M.4    Schachtman, D.P.5
  • 60
    • 33845966427 scopus 로고    scopus 로고
    • The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins
    • 16990282
    • Sottocornola B. Visconti S. Orsi S. Gazzarrini S. Giacometti S. Olivari C. et al. (2006). The potassium channel KAT1 is activated by plant and animal 14-3-3 proteins. J. Biol. Chem. 281, 35735–35741. 10.1074/jbc.M60336120016990282
    • (2006) J. Biol. Chem , vol.281 , pp. 35735-35741
    • Sottocornola, B.1    Visconti, S.2    Orsi, S.3    Gazzarrini, S.4    Giacometti, S.5    Olivari, C.6
  • 61
    • 43249124511 scopus 로고    scopus 로고
    • Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis
    • 18463617
    • Sugiyama N. Nakagami H. Mochida K. Daudi A. Tomita M. Shirasu K. et al. (2008). Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis. Mol. Syst. Biol. 4, 193. 10.1038/msb.2008.3218463617
    • (2008) Mol. Syst. Biol , vol.4 , pp. 193
    • Sugiyama, N.1    Nakagami, H.2    Mochida, K.3    Daudi, A.4    Tomita, M.5    Shirasu, K.6
  • 62
    • 80052475187 scopus 로고    scopus 로고
    • The 14-3-3 isoforms chi and epsilon differentially bind client proteins from developing Arabidopsis seed
    • 21766784
    • Swatek K. N. Graham K. Agrawal G. K. Thelen J. J. (2011). The 14-3-3 isoforms chi and epsilon differentially bind client proteins from developing Arabidopsis seed. J. Proteome Res. 10, 4076–4087. 10.1021/pr200263m21766784
    • (2011) J. Proteome Res , vol.10 , pp. 4076-4087
    • Swatek, K.N.1    Graham, K.2    Agrawal, G.K.3    Thelen, J.J.4
  • 63
    • 84896133428 scopus 로고    scopus 로고
    • Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases
    • 24438037
    • Swatek K. N. Wilson R. S. Ahsan N. Tritz R. L. Thelen J. J. (2014). Multisite phosphorylation of 14-3-3 proteins by calcium-dependent protein kinases. Biochem. J. 459, 15–25. 10.1042/BJ2013003524438037
    • (2014) Biochem. J , vol.459 , pp. 15-25
    • Swatek, K.N.1    Wilson, R.S.2    Ahsan, N.3    Tritz, R.L.4    Thelen, J.J.5
  • 64
    • 80051949849 scopus 로고    scopus 로고
    • 14-3-3 proteins act as intracellular receptors for rice Hd3a florigen
    • 21804566
    • Taoka K. Ohki I. Tsuji H. Furuita K. Hayashi K. Yanase T. et al. (2011). 14-3-3 proteins act as intracellular receptors for rice Hd3a florigen. Nature 476, 332–335. 10.1038/nature1027221804566
    • (2011) Nature , vol.476 , pp. 332-335
    • Taoka, K.1    Ohki, I.2    Tsuji, H.3    Furuita, K.4    Hayashi, K.5    Yanase, T.6
  • 65
    • 77950361848 scopus 로고    scopus 로고
    • The Arabidopsis rcn1-1 mutation impairs dephosphorylation of Phot2, resulting in enhanced blue light responses
    • 20139163
    • Tseng T. S. Briggs W. R. (2010). The Arabidopsis rcn1-1 mutation impairs dephosphorylation of Phot2, resulting in enhanced blue light responses. Plant Cell 22, 392–402. 10.1105/tpc.109.06642320139163
    • (2010) Plant Cell , vol.22 , pp. 392-402
    • Tseng, T.S.1    Briggs, W.R.2
  • 66
    • 84860180213 scopus 로고    scopus 로고
    • The role of a 14-3-3 protein in stomatal opening mediated by PHOT2 in Arabidopsis
    • 22408078
    • Tseng T. S. Whippo C. Hangarter R. P. Briggs W. R. (2012). The role of a 14-3-3 protein in stomatal opening mediated by PHOT2 in Arabidopsis. Plant Cell 24, 1114–1126. 10.1105/tpc.111.09213022408078
    • (2012) Plant Cell , vol.24 , pp. 1114-1126
    • Tseng, T.S.1    Whippo, C.2    Hangarter, R.P.3    Briggs, W.R.4
  • 67
    • 0028948289 scopus 로고
    • The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue
    • 7744048
    • van Heusden G. P. Griffiths D. J. Ford J. C. Chin A. W. T. F. Schrader P. A. Carr A. M. et al. (1995). The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue. Eur. J. Biochem. 229, 45–53. 10.1111/j.1432-1033.1995.0045l.x7744048
    • (1995) Eur. J. Biochem , vol.229 , pp. 45-53
    • van Heusden, G.P.1    Griffiths, D.J.2    Ford, J.C.3    Chin, A.W.T.F.4    Schrader, P.A.5    Carr, A.M.6
  • 68
    • 84913570631 scopus 로고    scopus 로고
    • Higher order Arabidopsis 14-3-3 mutants show 14-3-3 involvement in primary root growth both under control and abiotic stress conditions
    • 25189593
    • van Kleeff P. J. Jaspert N. Li K. W. Rauch S. Oecking C. de Boer A. H. (2014). Higher order Arabidopsis 14-3-3 mutants show 14-3-3 involvement in primary root growth both under control and abiotic stress conditions. J. Exp. Bot. 65, 5877–5888. 10.1093/jxb/eru33825189593
    • (2014) J. Exp. Bot , vol.65 , pp. 5877-5888
    • van Kleeff, P.J.1    Jaspert, N.2    Li, K.W.3    Rauch, S.4    Oecking, C.5    de Boer, A.H.6
  • 69
    • 40349091686 scopus 로고    scopus 로고
    • An “Electronic Fluorescent Pictograph” browser for exploring and analyzing large-scale biological data sets
    • 17684564
    • Winter D. Vinegar B. Nahal H. Ammar R. Wilson G. V. Provart N. J. (2007). An “Electronic Fluorescent Pictograph” browser for exploring and analyzing large-scale biological data sets. PLoS ONE 2:e718. 10.1371/journal.pone.000071817684564
    • (2007) PLoS ONE , vol.2 , pp. e718
    • Winter, D.1    Vinegar, B.2    Nahal, H.3    Ammar, R.4    Wilson, G.V.5    Provart, N.J.6
  • 70
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3:phosphopeptide binding specificity
    • 9428519
    • Yaffe M. B. Rittinger K. Volinia S. Caron P. R. Aitken A. Leffers H. et al. (1997). The structural basis for 14-3-3:phosphopeptide binding specificity. Cell 91, 961–971. 9428519
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1    Rittinger, K.2    Volinia, S.3    Caron, P.R.4    Aitken, A.5    Leffers, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.