메뉴 건너뛰기




Volumn 3, Issue 7, 2002, Pages

The 14-3-3s

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; DIMER; ISOPROTEIN; PROTEIN 14 3 3; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0036378769     PISSN: 14656906     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (141)

References (40)
  • 1
    • 0001954475 scopus 로고
    • Specific acidic proteins of the nervous system
    • Edited by Carlson FD. Englewood Cliffs, NJ: Prentice-Hall
    • Moore B, Perez V: Specific acidic proteins of the nervous system. In Physiological and Biochemical Aspects of Nervous Integration. Edited by Carlson FD. Englewood Cliffs, NJ: Prentice-Hall; 1967: 343-359.
    • (1967) Physiological and Biochemical Aspects of Nervous Integration , pp. 343-359
    • Moore, B.1    Perez, V.2
  • 3
    • 0026437586 scopus 로고
    • Brain proteins in plants: An Arabidopsis homolog to neurotransmitter pathway activators is part of a DNA binding complex
    • Lu G, DeLisle AJ, de Vetten NC, Ferl RJ: Brain proteins in plants: an Arabidopsis homolog to neurotransmitter pathway activators is part of a DNA binding complex. Proc Natl Acad Sci USA 1992, 89:11490-11494.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11490-11494
    • Lu, G.1    DeLisle, A.J.2    de Vetten, N.C.3    Ferl, R.J.4
  • 4
    • 0026938875 scopus 로고
    • A maize protein associated with the G-box binding complex has homology to brain regulatory proteins
    • de Vetten NC, Lu G, Ferl RJ: A maize protein associated with the G-box binding complex has homology to brain regulatory proteins. Plant Cell 1992, 4:1295-1307.
    • (1992) Plant Cell , vol.4 , pp. 1295-1307
    • de Vetten, N.C.1    Lu, G.2    Ferl, R.J.3
  • 5
    • 0034788964 scopus 로고    scopus 로고
    • 14-3-3 proteins: Key regulators of cell division, signalling and apoptosis
    • van Hemert, M. J., Steensma, H. Y, van Heusden, G. P: 14-3-3 proteins: key regulators of cell division, signalling and apoptosis. BioEssays 2001, 23:936-946.
    • (2001) BioEssays , vol.23 , pp. 936-946
    • van Hemert, M.J.1    Steensma, H.Y.2    van Heusden, G.P.3
  • 6
    • 0032837907 scopus 로고    scopus 로고
    • The 14-3-3 proteins: Cellular regulators of plant metabolism
    • Chung HJ, Sehnke PC, Ferl RJ: The 14-3-3 proteins: cellular regulators of plant metabolism. Trends Plant Sci 1999, 4:367-371.
    • (1999) Trends Plant Sci , vol.4 , pp. 367-371
    • Chung, H.J.1    Sehnke, P.C.2    Ferl, R.J.3
  • 7
    • 0034969736 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 family of signaling regulators
    • DeLille JM, Sehnke PC, Ferl RJ: The Arabidopsis 14-3-3 family of signaling regulators. Plant Physiol 2001, 126:35-38.
    • (2001) Plant Physiol , vol.126 , pp. 35-38
    • DeLille, J.M.1    Sehnke, P.C.2    Ferl, R.J.3
  • 8
    • 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 RJ, Sommarin M, Larsson C: Evolution of the 14-3-3 protein family: does the large number of isoforms in multicellular organisms reflect functional specificity? J Mol Evol 2000, 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
  • 10
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS: Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 1996, 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 12
    • 0032512413 scopus 로고    scopus 로고
    • Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews RK, Harris SJ, McNally T, Berndt MC: Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. Biochemistry 1998, 37:638-647.
    • (1998) Biochemistry , vol.37 , pp. 638-647
    • Andrews, R.K.1    Harris, S.J.2    McNally, T.3    Berndt, M.C.4
  • 13
    • 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 SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC: 14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove. J Biol Chem 1998, 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
  • 14
    • 0036277421 scopus 로고    scopus 로고
    • Consummating signal transduction: The role of 14-3-3 proteins in completion of signal-induced transitions in protein activity
    • Sehnke PC, DeLille JM, Ferl RJ: Consummating signal transduction: the role of 14-3-3 proteins in completion of signal-induced transitions in protein activity. Plant Cell 2002, 14:S339-S354.
    • (2002) Plant Cell , vol.14
    • Sehnke, P.C.1    DeLille, J.M.2    Ferl, R.J.3
  • 16
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
    • Xiao B, Smerdon SJ, Jones DH, Dodson GG, Soneji Y, Aitken A, Gamblin SJ: Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 1995, 376:188-191.
    • (1995) Nature , vol.376 , pp. 188-191
    • Xiao, B.1    Smerdon, S.J.2    Jones, D.H.3    Dodson, G.G.4    Soneji, Y.5    Aitken, A.6    Gamblin, S.J.7
  • 17
    • 0030827138 scopus 로고    scopus 로고
    • Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPHI with 14-3-3beta protein
    • Zhang SH, Kobayashi R, Graves PR, Piwnica-Worms H, Tonks NK: Serine phosphorylation-dependent association of the band 4.1-related protein-tyrosine phosphatase PTPHI with 14-3-3beta protein. J Biol Chem 1997, 272:27281-27287.
    • (1997) J. Biol. Chem , vol.272 , pp. 27281-27287
    • Zhang, S.H.1    Kobayashi, R.2    Graves, P.R.3    Piwnica-Worms, H.4    Tonks, N.K.5
  • 18
    • 0032568944 scopus 로고    scopus 로고
    • Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase
    • Wang H, Zhang L, Liddington R, Fu H: Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase. J Biol Chem 1998, 273: 16297-16304.
    • (1998) J. Biol. Chem , vol.273 , pp. 16297-16304
    • Wang, H.1    Zhang, L.2    Liddington, R.3    Fu, H.4
  • 21
    • 0029067231 scopus 로고
    • Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: Implications for function as adapter proteins
    • Jones DH, Ley S, Aitken A: Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins. FEBS Lett 1995, 368:55-58.
    • (1995) FEBS Lett , vol.368 , pp. 55-58
    • Jones, D.H.1    Ley, S.2    Aitken, A.3
  • 22
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • Rittinger K, Budman J, Xu J, Volinia S, Cantley LC, Smerdon SJ, Gamblin SJ, Yaffe MB: Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell 1999, 4: 153-166.
    • (1999) Mol. Cell , vol.4 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 23
    • 0031463930 scopus 로고    scopus 로고
    • Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize
    • Bihn EA, Paul AL, Wang SW, Erdos GW, Ferl RJ: Localization of 14-3-3 proteins in the nuclei of Arabidopsis and maize. Plant J 1997, 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
  • 24
    • 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 PC, Henry R, Cline K, Ferl RJ: 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 2000, 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
  • 25
    • 0030220501 scopus 로고    scopus 로고
    • Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene
    • Daugherty CJ, Rooney MF, Miller PW, Ferl RJ: Molecular organization and tissue-specific expression of an Arabidopsis 14-3-3 gene. Plant Cell 1996, 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
  • 26
    • 0035895274 scopus 로고    scopus 로고
    • Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
    • Sehnke PC, Chung HJ, Wu K, Ferl RJ: Regulation of starch accumulation by granule-associated plant 14-3-3 proteins. Proc Natl Acad Sci USA 2001, 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
  • 27
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • Cutler SR, Ehrhardt DW, Griffitts JS, Somerville CR: Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency. Proc Natl Acad Sci USA 2000, 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
  • 29
    • 0033552943 scopus 로고    scopus 로고
    • Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein
    • Lopez-Girona A, Furnari B, Mondesert O, Russell P: Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 1999, 397: 172-175.
    • (1999) Nature , vol.397 , pp. 172-175
    • Lopez-Girona, A.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 30
    • 0010442083 scopus 로고    scopus 로고
    • Sequences of five Arabidopsis general regulatory factor (GRF) genes encoding 14-3-3 proteins
    • Chung H-J, Shanker S, Ferl RJ: Sequences of five Arabidopsis general regulatory factor (GRF) genes encoding 14-3-3 proteins. Plant Physiol 1999, 120:1206.
    • (1999) Plant Physiol , vol.120 , pp. 1206
    • Chung, H.-J.1    Shanker, S.2    Ferl, R.J.3
  • 31
    • 0030581305 scopus 로고    scopus 로고
    • Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption
    • van Heusden GP, van der Zanden AL, Ferl RJ, Steensma HY: Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption. FEBS Lett 1996, 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
  • 32
    • 0030822692 scopus 로고    scopus 로고
    • Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function
    • Broadie K, Rushton E, Skoulakis EM, Davis RL: Leonardo, a Drosophila 14-3-3 protein involved in learning, regulates presynaptic function. Neuron 1997, 19:391-402.
    • (1997) Neuron , vol.19 , pp. 391-402
    • Broadie, K.1    Rushton, E.2    Skoulakis, E.M.3    Davis, R.L.4
  • 33
    • 0030999664 scopus 로고    scopus 로고
    • 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila
    • Chang HC, Rubin GM: 14-3-3 epsilon positively regulates Ras-mediated signaling in Drosophila. Genes Dev 1997, 11:1132-1139.
    • (1997) Genes Dev , vol.11 , pp. 1132-1139
    • Chang, H.C.1    Rubin, G.M.2
  • 34
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
    • Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ: Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 1996, 87: 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 35
    • 0030611095 scopus 로고    scopus 로고
    • Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216
    • Peng CY, Graves PR, Thoma RS, Wu Z, Shaw AS, Piwnica-Worms H: Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216. Science 1997, 277:1501-1505.
    • (1997) Science , vol.277 , pp. 1501-1505
    • Peng, C.Y.1    Graves, P.R.2    Thoma, R.S.3    Wu, Z.4    Shaw, A.S.5    Piwnica-Worms, H.6
  • 36
    • 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 JL, Athwal GS, Wu K, Ferl RJ, Huber SC: 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 1996, 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
  • 37
    • 0010486628 scopus 로고    scopus 로고
    • Entrez nucleotide view
    • Entrez nucleotide view [http://www.ncbi.nih.gov/entrez/query.fcgi]
  • 38
    • 0010492162 scopus 로고    scopus 로고
    • The laboratory of Robert J. Ferl
    • The laboratory of Robert J. Ferl [http://www.hos.ufl.edu/ferllab/]
  • 39
    • 0027968068 scopus 로고
    • Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ: Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N, Nei M: The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4:406-425.
    • (1987) Mol. Biol. Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.