메뉴 건너뛰기




Volumn 16, Issue 4, 2005, Pages 1735-1743

Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL AGENT; HYBRID PROTEIN; ISOPROTEIN; PEPTIDE;

EID: 16344373193     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-09-0839     Document Type: Article
Times cited : (93)

References (74)
  • 1
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 and its possible role in co-ordinating multiple signalling pathways
    • Aitken, A. (1996). 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol. 6, 341-347.
    • (1996) Trends Cell Biol. , vol.6 , pp. 341-347
    • Aitken, A.1
  • 2
    • 0036914288 scopus 로고    scopus 로고
    • Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants
    • Aitken, A. (2002). Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants. Plant Mol. Biol. 50, 993-1010.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 993-1010
    • Aitken, A.1
  • 4
    • 7944234552 scopus 로고    scopus 로고
    • Plasma membrane H(+)-ATPase and 14-3-3 isoforms of Arabidopsis leaves: Evidence for isoform specificity in the 14-3-3/H(+)-ATPase interaction
    • Alsterfjord, M., Sehnke, P. C., Arkell, A., Larsson, H., Svennelid, F., Rosenquist, M., Ferl, R. J., Sommarin, M., and Larsson, C. (2004). Plasma membrane H(+)-ATPase and 14-3-3 isoforms of Arabidopsis leaves: evidence for isoform specificity in the 14-3-3/H(+)-ATPase interaction. Plant Cell Physiol. 45, 1202-1210.
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1202-1210
    • Alsterfjord, M.1    Sehnke, P.C.2    Arkell, A.3    Larsson, H.4    Svennelid, F.5    Rosenquist, M.6    Ferl, R.J.7    Sommarin, M.8    Larsson, C.9
  • 5
    • 0032197397 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an amp-binding site on 14-3-3 proteins
    • Athwal, G. S., Huber, J. L., and Huber, S. C. (1998). Phosphorylated nitrate reductase and 14-3-3 proteins. Site of interaction, effects of ions, and evidence for an amp-binding site on 14-3-3 proteins. Plant Physiol. 118, 1041-1048.
    • (1998) Plant Physiol. , vol.118 , pp. 1041-1048
    • Athwal, G.S.1    Huber, J.L.2    Huber, S.C.3
  • 6
    • 0033848997 scopus 로고    scopus 로고
    • Involvement of 14-3-3 proteins in the osmotic regulation of H+-ATPase in plant plasma membranes
    • Babakov, A. V., Chelysheva, V. V., Klychnikov, O. I., Zorinyanz, S. E., Trofimova, M. S., and De Boer, A. H. (2000). Involvement of 14-3-3 proteins in the osmotic regulation of H+-ATPase in plant plasma membranes. Planta 211, 446-448.
    • (2000) Planta , vol.211 , pp. 446-448
    • Babakov, A.V.1    Chelysheva, V.V.2    Klychnikov, O.I.3    Zorinyanz, S.E.4    Trofimova, M.S.5    De Boer, A.H.6
  • 7
    • 0030602179 scopus 로고    scopus 로고
    • 14-3-3 Proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases
    • Bachmann, M., Huber, J. L., Athwal, G. S., Wu, K., Ferl, R. J., and Huber, S. C. (1996). 14-3-3 proteins associate with the regulatory phosphorylation site of spinach leaf nitrate reductase in an isoform-specific manner and reduce dephosphorylation of Ser-543 by endogenous protein phosphatases. FEBS Lett. 398, 26-30.
    • (1996) FEBS Lett. , vol.398 , pp. 26-30
    • Bachmann, M.1    Huber, J.L.2    Athwal, G.S.3    Wu, K.4    Ferl, R.J.5    Huber, S.C.6
  • 8
    • 0031624102 scopus 로고    scopus 로고
    • In planta Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration
    • Bechtold, N., and Pelletier, G. (1998). In planta Agrobacterium-mediated transformation of adult Arabidopsis thaliana plants by vacuum infiltration. Methods Mol. Biol. 82, 259-266.
    • (1998) Methods Mol. Biol. , vol.82 , pp. 259-266
    • Bechtold, N.1    Pelletier, G.2
  • 9
    • 0031463930 scopus 로고    scopus 로고
    • Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize
    • Bihn, E. A., Paul, A. L., Wang, S. W., Erdos, G. W., and Ferl, R. J. (1997). Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize. Plant J. 12, 1439-1445.
    • (1997) Plant J. , vol.12 , pp. 1439-1445
    • Bihn, E.A.1    Paul, A.L.2    Wang, S.W.3    Erdos, G.W.4    Ferl, R.J.5
  • 10
    • 0032874346 scopus 로고    scopus 로고
    • Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice
    • Bodendorf, U., Cziepluch, C., Jauniaux, J. C., Rommelaere, J., and Salome, N. (1999). Nuclear export factor CRM1 interacts with nonstructural proteins NS2 from parvovirus minute virus of mice. J. Virol. 73, 7769-7779.
    • (1999) J. Virol. , vol.73 , pp. 7769-7779
    • Bodendorf, U.1    Cziepluch, C.2    Jauniaux, J.C.3    Rommelaere, J.4    Salome, N.5
  • 12
    • 0035957331 scopus 로고    scopus 로고
    • 14-3-3 Protein is a regulator of the mitochondrial and chloroplast ATP synthase
    • Bunney, T. D., van Walraven, H. S., and de Boer, A. H. (2001). 14-3-3 protein is a regulator of the mitochondrial and chloroplast ATP synthase. Proc. Natl. Acad. Sci. USA 98, 4249-4254.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4249-4254
    • Bunney, T.D.1    Van Walraven, H.S.2    De Boer, A.H.3
  • 13
    • 0037064013 scopus 로고    scopus 로고
    • The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307
    • Callejo, M., Alvarez, D., Price, G. B., and Zannis-Hadjopoulos, M. (2002). The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307. J. Biol. Chem. 277, 38416-38423.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38416-38423
    • Callejo, M.1    Alvarez, D.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 14
    • 0035943652 scopus 로고    scopus 로고
    • Adenosine 5′-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H(+)-ATPase
    • Camoni, L., Visconti, S., Marra, M., and Aducci, P. (2001). Adenosine 5′-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H(+)-ATPase. J. Biol. Chem. 276, 31709-31712.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31709-31712
    • Camoni, L.1    Visconti, S.2    Marra, M.3    Aducci, P.4
  • 15
    • 0030999664 scopus 로고    scopus 로고
    • 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila
    • Chang, H. C., and Rubin, G. M. (1997). 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila. Genes Dev. 11, 1132-1139.
    • (1997) Genes Dev. , vol.11 , pp. 1132-1139
    • Chang, H.C.1    Rubin, G.M.2
  • 16
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::xDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • Cutler, S. R., Ehrhardt, D. W., Griffitts, J. S., and Somerville, C. R. (2000). Random GFP::xDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc. Natl. Acad. Sci. USA 97, 3718-3723.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 17
    • 0036926903 scopus 로고    scopus 로고
    • Starch biosynthesis during pollen maturation is associated with altered patterns of gene expression in maize
    • Datta, R., Chamusco, K. C., and Chourey, P. S. (2002). Starch biosynthesis during pollen maturation is associated with altered patterns of gene expression in maize. Plant Physiol. 130, 1645-1656.
    • (2002) Plant Physiol. , vol.130 , pp. 1645-1656
    • Datta, R.1    Chamusco, K.C.2    Chourey, P.S.3
  • 18
    • 0030220501 scopus 로고    scopus 로고
    • Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene
    • Daugherty, C. J., Rooney, M. F., Miller, P. W., and Ferl, R. J. (1996). Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene. Plant Cell 8, 1239-1248.
    • (1996) Plant Cell , vol.8 , pp. 1239-1248
    • Daugherty, C.J.1    Rooney, M.F.2    Miller, P.W.3    Ferl, R.J.4
  • 19
    • 0028676253 scopus 로고
    • Two genes encoding GF14 (14-3-3) proteins in Zed mays. Structure, expression, and potential regulation by the G-box binding complex
    • de Vetten, N. C., and Ferl, R. J. (1994). Two genes encoding GF14 (14-3-3) proteins in Zed mays. Structure, expression, and potential regulation by the G-box binding complex. Plant Physiol. 106, 1593-1604.
    • (1994) Plant Physiol. , vol.106 , pp. 1593-1604
    • De Vetten, N.C.1    Ferl, R.J.2
  • 20
    • 0034969736 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 family of signaling regulators
    • DeLille, J. M., Sehnke, P. C., and Ferl, R. J. (2001). The Arabidopsis 14-3-3 family of signaling regulators. Plant Physiol. 126, 35-38.
    • (2001) Plant Physiol. , vol.126 , pp. 35-38
    • DeLille, J.M.1    Sehnke, P.C.2    Ferl, R.J.3
  • 21
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty, M. K., and Morrison, D. K. (2004). Unlocking the code of 14-3-3. J. Cell Sci. 117, 1875-1884.
    • (2004) J. Cell Sci. , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 22
    • 0036893516 scopus 로고    scopus 로고
    • A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex
    • Eilers, A. L., Sundwall, E., Lin, M., Sullivan, A. A., and Ayer, D. E. (2002). A novel heterodimerization domain, CRM1, and 14-3-3 control subcellular localization of the MondoA-Mlx heterocomplex. Mol. Cell. Biol. 22, 8514-8526.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8514-8526
    • Eilers, A.L.1    Sundwall, E.2    Lin, M.3    Sullivan, A.A.4    Ayer, D.E.5
  • 27
    • 0041707637 scopus 로고    scopus 로고
    • 14-3-3 Acts as an intramolecular bridge to regulate cdc25B localization and activity
    • Giles, N., Forrest, A., and Gabrielli, B. (2003). 14-3-3 acts as an intramolecular bridge to regulate cdc25B localization and activity. J. Biol. Chem. 278, 28580-28587.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28580-28587
    • Giles, N.1    Forrest, A.2    Gabrielli, B.3
  • 28
    • 0034608955 scopus 로고    scopus 로고
    • Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization
    • Grozinger, C. M., and Schreiber, S. L. (2000). Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. Proc. Natl. Acad. Sci. USA 97, 7835-7840.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7835-7840
    • Grozinger, C.M.1    Schreiber, S.L.2
  • 29
    • 0035905757 scopus 로고    scopus 로고
    • Identification of a novel interaction between integrin beta1 and 14-3-3beta
    • Han, D. C., Rodriguez, L. G., and Guan, J. L. (2001). Identification of a novel interaction between integrin beta1 and 14-3-3beta. Oncogene 20, 346-357.
    • (2001) Oncogene , vol.20 , pp. 346-357
    • Han, D.C.1    Rodriguez, L.G.2    Guan, J.L.3
  • 30
    • 0030435802 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide riboside activates nitrate reductase in darkened spinach and pea leaves
    • Huber, S. C., and Kaiser, W. M. (1996). 5-Aminoimidazole-4-carboxamide riboside activates nitrate reductase in darkened spinach and pea leaves. Physiol. Plant 98, 833-837.
    • (1996) Physiol. Plant , vol.98 , pp. 833-837
    • Huber, S.C.1    Kaiser, W.M.2
  • 31
    • 0036914587 scopus 로고    scopus 로고
    • Metabolic enzymes as targets for 14-3-3 proteins
    • Huber, S. C., MacKintosh, C., and Kaiser, W. M. (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
  • 32
    • 4344598183 scopus 로고    scopus 로고
    • Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization
    • Jin, J., et al. (2004). Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. Curr. Biol. 24, 1436-1450.
    • (2004) Curr. Biol. , vol.24 , pp. 1436-1450
    • Jin, J.1
  • 33
    • 17744380191 scopus 로고    scopus 로고
    • TAZ: A novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins
    • Kanai, F., et al. (2000). TAZ: a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ domain proteins. EMBO J. 19, 6778-6791.
    • (2000) EMBO J. , vol.19 , pp. 6778-6791
    • Kanai, F.1
  • 34
    • 0030953744 scopus 로고    scopus 로고
    • Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development
    • Kockel, L., Vorbruggen, G., Jackle, H., Mlodzik, M., and Bohmann, D. (1997). Requirement for Drosophila 14-3-3 zeta in Raf-dependent photoreceptor development. Genes Dev. 11, 1140-1147.
    • (1997) Genes Dev. , vol.11 , pp. 1140-1147
    • Kockel, L.1    Vorbruggen, G.2    Jackle, H.3    Mlodzik, M.4    Bohmann, D.5
  • 35
    • 0034623092 scopus 로고    scopus 로고
    • Members of the Arabidopsis 14-3-3 gene family trans-complement two types of defects in fission yeast
    • Kuromori, T., and Yamamoto, M. (2000). Members of the Arabidopsis 14-3-3 gene family trans-complement two types of defects in fission yeast. Plant Sci. 158, 155-161.
    • (2000) Plant Sci. , vol.158 , pp. 155-161
    • Kuromori, T.1    Yamamoto, M.2
  • 36
    • 0035158899 scopus 로고    scopus 로고
    • Positive regulation of Weel by Chk1 and 14-3-3 proteins
    • Lee, J., Kumagai, A., and Dunphy, W. G. (2001). Positive regulation of Weel by Chk1 and 14-3-3 proteins. Mol. Biol. Cell 12, 551-563.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 551-563
    • Lee, J.1    Kumagai, A.2    Dunphy, W.G.3
  • 37
    • 0030139810 scopus 로고    scopus 로고
    • Transcription factor veracity: Is GBF3 responsible for ABA-regulated expression of Arabidopsis Adh?
    • Lu, G., Paul, A. L., McCarty, D. R., and Ferl, R. J. (1996). Transcription factor veracity: is GBF3 responsible for ABA-regulated expression of Arabidopsis Adh? Plant Cell 8, 847-857.
    • (1996) Plant Cell , vol.8 , pp. 847-857
    • Lu, G.1    Paul, A.L.2    McCarty, D.R.3    Ferl, R.J.4
  • 38
    • 0035109584 scopus 로고    scopus 로고
    • Increased glutamine synthetase activity and changes in amino acid pools in leaves treated with 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR)
    • Man, H. M., and Kaiser, W. M. (2001). Increased glutamine synthetase activity and changes in amino acid pools in leaves treated with 5-aminoimidazole-4-carboxiamide ribonucleoside (AICAR). Physiol. Plant 111, 291-296.
    • (2001) Physiol. Plant , vol.111 , pp. 291-296
    • Man, H.M.1    Kaiser, W.M.2
  • 39
    • 0242501000 scopus 로고    scopus 로고
    • 14-3-3 isoforms and pattern formation during barley microspore embryogenesis
    • Maraschin, S.D.F., Lamers, G. E., de Pater, B. S., Spaink, H. P., and Wang, M. (2003). 14-3-3 isoforms and pattern formation during barley microspore embryogenesis. J. Exp. Bot. 54, 1033-1043.
    • (2003) J. Exp. Bot. , vol.54 , pp. 1033-1043
    • Maraschin, S.D.F.1    Lamers, G.E.2    De Pater, B.S.3    Spaink, H.P.4    Wang, M.5
  • 40
    • 3543150636 scopus 로고    scopus 로고
    • The subcellular localization of the ChoRE-binding protein, encoded by the Williams-Beuren syndrome critical region gene 14, is regulated by 14-3-3
    • Merla, G., Howald, C., Antonarakis, S. E., and Reymond, A. (2004). The subcellular localization of the ChoRE-binding protein, encoded by the Williams-Beuren syndrome critical region gene 14, is regulated by 14-3-3. Hum. Mol. Genet. 13, 1505-1514.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1505-1514
    • Merla, G.1    Howald, C.2    Antonarakis, S.E.3    Reymond, A.4
  • 41
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A. J., and Xing, H. (2000). 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell Signal 12, 703-709.
    • (2000) Cell Signal , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 42
    • 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
    • Pan, S., Sehnke, P. C., Ferl, R. J., and 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.
    • (1999) Plant Cell , vol.11 , pp. 1591-1602
    • Pan, S.1    Sehnke, P.C.2    Ferl, R.J.3    Gurley, W.B.4
  • 43
    • 0034979886 scopus 로고    scopus 로고
    • Transgene expression patterns indicate that spaceflight affects stress signal perception and transduction in Arabidopsis
    • Paul, A. L., Daugherty, C. J., Bihn, E. A., Chapman, D. K., Norwood, K. L., and Ferl, R. J. (2001). Transgene expression patterns indicate that spaceflight affects stress signal perception and transduction in Arabidopsis. Plant Physiol. 126, 613-621.
    • (2001) Plant Physiol. , vol.126 , pp. 613-621
    • Paul, A.L.1    Daugherty, C.J.2    Bihn, E.A.3    Chapman, D.K.4    Norwood, K.L.5    Ferl, R.J.6
  • 44
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., Masters, S. C., Bankston, L. A., Pohl, J., Wang, B., Fu, H., and Liddington, R. C. (1998). 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J. Biol. Chem. 273, 16305-16310.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16305-16310
    • Petosa, C.1    Masters, S.C.2    Bankston, L.A.3    Pohl, J.4    Wang, B.5    Fu, H.6    Liddington, R.C.7
  • 45
    • 0035503073 scopus 로고    scopus 로고
    • Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo
    • Philip, N., Acevedo, S. F., and Skoulakis, E. M. (2001). Conditional rescue of olfactory learning and memory defects in mutants of the 14-3-3zeta gene leonardo. J. Neurosci. 21, 8417-8425.
    • (2001) J. Neurosci. , vol.21 , pp. 8417-8425
    • Philip, N.1    Acevedo, S.F.2    Skoulakis, E.M.3
  • 47
    • 0036785555 scopus 로고    scopus 로고
    • Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins
    • Prymakowska-Bosak, M., Hock, R., Catez, F., Lim, J. H., Birger, Y., Shirakawa, H., Lee, K., and Bustin, M. (2002). Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins. Mol. Cell. Biol. 22, 6809-6819.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6809-6819
    • Prymakowska-Bosak, M.1    Hock, R.2    Catez, F.3    Lim, J.H.4    Birger, Y.5    Shirakawa, H.6    Lee, K.7    Bustin, M.8
  • 48
    • 11144256205 scopus 로고    scopus 로고
    • Isoform-specific expression of 14-3-3 proteins in human lung cancer tissues
    • Qi, W., Liu, X., Qiao, D., and Martinez, J. D. (2005). Isoform-specific expression of 14-3-3 proteins in human lung cancer tissues. Int. J. Cancer 113, 359-363.
    • (2005) Int. J. Cancer , vol.113 , pp. 359-363
    • Qi, W.1    Liu, X.2    Qiao, D.3    Martinez, J.D.4
  • 49
    • 0034644733 scopus 로고    scopus 로고
    • Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins
    • Qiu, W., Zhuang, S., von Lintig, F. C., Boss, G. R., and Pilz, R. B. (2000). Cell type-specific regulation of B-Raf kinase by cAMP and 14-3-3 proteins. J. Biol. Chem. 275, 31921-31929.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31921-31929
    • Qiu, W.1    Zhuang, S.2    Von Lintig, F.C.3    Boss, G.R.4    Pilz, R.B.5
  • 50
    • 0033719624 scopus 로고    scopus 로고
    • Evolution of the 14-3-3 protein family: Does the large number of isoforms in multicellular organisms reflect functional specificity?
    • Rosenquist, M., Sehnke, P., Ferl, R. J., Sommarin, M., and Larsson, C. (2000). Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity? J. Mol. Evol. 51, 446-458.
    • (2000) J. Mol. Evol. , vol.51 , pp. 446-458
    • Rosenquist, M.1    Sehnke, P.2    Ferl, R.J.3    Sommarin, M.4    Larsson, C.5
  • 51
    • 0032752399 scopus 로고    scopus 로고
    • Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
    • Roth, D., Birkenfeld, J., and Betz, H. (1999). Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett. 460, 411-416.
    • (1999) FEBS Lett. , vol.460 , pp. 411-416
    • Roth, D.1    Birkenfeld, J.2    Betz, H.3
  • 52
    • 0032076829 scopus 로고    scopus 로고
    • 14-3-3 Proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1
    • Schultz, T. F., Medina, J., Hill, A., and Quatrano, R. S. (1998). 14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1. Plant Cell 10, 837-847.
    • (1998) Plant Cell , vol.10 , pp. 837-847
    • Schultz, T.F.1    Medina, J.2    Hill, A.3    Quatrano, R.S.4
  • 53
    • 0035895274 scopus 로고    scopus 로고
    • Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
    • Sehnke, P. C., Chung, H. J., Wu, K., and Ferl, R. J. (2001). Regulation of starch accumulation by granule-associated plant 14-3-3 proteins. Proc. Natl. Acad. Sci. USA 98, 765-770.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 765-770
    • Sehnke, P.C.1    Chung, H.J.2    Wu, K.3    Ferl, R.J.4
  • 54
    • 0033759068 scopus 로고    scopus 로고
    • Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma
    • Sehnke, P. C., Henry, R., Cline, K., and Ferl, R. J. (2000). Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma. Plant Physiol. 122, 235-242.
    • (2000) Plant Physiol. , vol.122 , pp. 235-242
    • Sehnke, P.C.1    Henry, R.2    Cline, K.3    Ferl, R.J.4
  • 57
    • 0035890044 scopus 로고    scopus 로고
    • Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis
    • Subramanian, R. R., Masters, S. C., Zhang, H., and Fu, H. (2001). Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis. Exp. Cell Res. 271, 142-151.
    • (2001) Exp. Cell Res. , vol.271 , pp. 142-151
    • Subramanian, R.R.1    Masters, S.C.2    Zhang, H.3    Fu, H.4
  • 58
    • 1542328926 scopus 로고    scopus 로고
    • Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins
    • Subramanian, R. R., Zhang, H., Wang, H., Ichijo, H., Miyashita, T., and Fu, H. (2004). Interaction of apoptosis signal-regulating kinase 1 with isoforms of 14-3-3 proteins. Exp. Cell Res. 294, 581-591.
    • (2004) Exp. Cell Res. , vol.294 , pp. 581-591
    • Subramanian, R.R.1    Zhang, H.2    Wang, H.3    Ichijo, H.4    Miyashita, T.5    Fu, H.6
  • 60
    • 0032508671 scopus 로고    scopus 로고
    • Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins
    • Toroser, D., Athwal, G. S., and Huber, S. C. (1998). Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins. FEBS Lett. 435, 110-114.
    • (1998) FEBS Lett. , vol.435 , pp. 110-114
    • Toroser, D.1    Athwal, G.S.2    Huber, S.C.3
  • 61
    • 4344651089 scopus 로고    scopus 로고
    • Binding of 14-3-3beta but not 14-3-3sigma controls the cytoplasmic localization of CDC25B: Binding site preferences of 14-3-3 subtypes and the subcellular localization of CDC25B
    • Uchida, S., Kuma, A., Ohtsubo, M., Shimura, M., Hirata, M., Nakagama, H., Matsunaga, T., Ishizaka, Y., and Yamashita, K. (2004). Binding of 14-3-3beta but not 14-3-3sigma controls the cytoplasmic localization of CDC25B: binding site preferences of 14-3-3 subtypes and the subcellular localization of CDC25B. J. Cell Sci. 117, 3011-3020.
    • (2004) J. Cell Sci. , vol.117 , pp. 3011-3020
    • Uchida, S.1    Kuma, A.2    Ohtsubo, M.3    Shimura, M.4    Hirata, M.5    Nakagama, H.6    Matsunaga, T.7    Ishizaka, Y.8    Yamashita, K.9
  • 62
    • 2342441988 scopus 로고    scopus 로고
    • Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta
    • van Hemert, M. J., Niemantsverdriet, M., Schmidt, T., Backendorf, C., and Spaink, H. P. (2004). Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta. J. Cell Sci. 117, 1411-1420.
    • (2004) J. Cell Sci. , vol.117 , pp. 1411-1420
    • Van Hemert, M.J.1    Niemantsverdriet, M.2    Schmidt, T.3    Backendorf, C.4    Spaink, H.P.5
  • 63
    • 0030581305 scopus 로고    scopus 로고
    • Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption
    • van Heusden, G. P., van der Zanden, A. L., Ferl, R. J., and Steensma, H. Y. (1996). Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption. FEBS Lett. 391, 252-256.
    • (1996) FEBS Lett. , vol.391 , pp. 252-256
    • Van Heusden, G.P.1    Van Der Zanden, A.L.2    Ferl, R.J.3    Steensma, H.Y.4
  • 64
    • 0037067137 scopus 로고    scopus 로고
    • Characterisation of two 14-3-3 genes from Trichoderma reesei: Interactions with yeast secretory pathway components
    • Vasara, T., Keranen, S., Penttila, M., and Saloheimo, M. (2002). Characterisation of two 14-3-3 genes from Trichoderma reesei: interactions with yeast secretory pathway components. Biochim. Biophys. Acta 1590, 27-40.
    • (2002) Biochim. Biophys. Acta , vol.1590 , pp. 27-40
    • Vasara, T.1    Keranen, S.2    Penttila, M.3    Saloheimo, M.4
  • 65
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang, B., Yang, H., Liu, Y. C., Jelinek, T., Zhang, L., Ruoslahti, E., and Fu, H. (1999). Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38, 12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 66
    • 0034128641 scopus 로고    scopus 로고
    • Binding of 14-3-3beta to the carboxyl terminus of Weel increases Weel stability, kinase activity, and G2-M cell population
    • Wang, Y., Jacobs, C., Hook, K. E., Duan, H., Booher, R. N., and Sun, Y. (2000). Binding of 14-3-3beta to the carboxyl terminus of Weel increases Weel stability, kinase activity, and G2-M cell population. Cell Growth Differ. 11, 211-219.
    • (2000) Cell Growth Differ. , vol.11 , pp. 211-219
    • Wang, Y.1    Jacobs, C.2    Hook, K.E.3    Duan, H.4    Booher, R.N.5    Sun, Y.6
  • 67
    • 0032999455 scopus 로고    scopus 로고
    • 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves
    • Weiner, H., and Kaiser, W. M. (1999). 14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves. FEBS Lett. 455, 75-78.
    • (1999) FEBS Lett. , vol.455 , pp. 75-78
    • Weiner, H.1    Kaiser, W.M.2
  • 69
    • 0031106133 scopus 로고    scopus 로고
    • The heterologous interactions among plant 14-3-3 proteins and identification of regions that are important for dimerization
    • Wu, K., Lu, G., Sehnke, P., and Ferl, R. J. (1997a). The heterologous interactions among plant 14-3-3 proteins and identification of regions that are important for dimerization. Arch. Biochem. Biophys. 339, 2-8.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 2-8
    • Wu, K.1    Lu, G.2    Sehnke, P.3    Ferl, R.J.4
  • 70
    • 0031200784 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 multigene family
    • Wu, K., Rooney, M. F., and Ferl, R. J. (1997b). The Arabidopsis 14-3-3 multigene family. Plant Physiol. 114, 1421-1431.
    • (1997) Plant Physiol. , vol.114 , pp. 1421-1431
    • Wu, K.1    Rooney, M.F.2    Ferl, R.J.3
  • 71
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work?-Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. (2002). How do 14-3-3 proteins work?-Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513, 53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 72
    • 0037447231 scopus 로고    scopus 로고
    • 14-3-3 dimers probe the assembly status of multimeric membrane proteins
    • Yuan, H., Michelsen, K., and Schwappach, B. (2003). 14-3-3 dimers probe the assembly status of multimeric membrane proteins. Curr. Biol. 13, 638-646.
    • (2003) Curr. Biol. , vol.13 , pp. 638-646
    • Yuan, H.1    Michelsen, K.2    Schwappach, B.3
  • 73
    • 0032746942 scopus 로고    scopus 로고
    • DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding
    • Zeng, Y., and Piwnica-Worms, H. (1999). DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding. Mol. Cell. Biol. 19, 7410-7419.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7410-7419
    • Zeng, Y.1    Piwnica-Worms, H.2
  • 74
    • 2442483847 scopus 로고    scopus 로고
    • p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor
    • Zenke, F. T., Krendel, M., DerMardirossian, C., King, C. C., Bohl, B. P., and Bokoch, G. M. (2004). p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to GEF-H1, a microtubule-localized Rho exchange factor. J. Biol. Chem. 279, 18392-18400.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18392-18400
    • Zenke, F.T.1    Krendel, M.2    DerMardirossian, C.3    King, C.C.4    Bohl, B.P.5    Bokoch, G.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.