메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 205-215

Regulation of transcription by MAP kinase cascades

Author keywords

[No Author keywords available]

Indexed keywords

DNA; MITOGEN ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR;

EID: 0029935418     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(96)80067-6     Document Type: Article
Times cited : (1175)

References (95)
  • 2
    • 0028221043 scopus 로고
    • Signalling pathways initiated by receptor tyrosine kinases in Drosophila
    • Perrimon N: Signalling pathways initiated by receptor tyrosine kinases in Drosophila. Curr Opin Cell Biol 1994, 6:260-266.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 260-266
    • Perrimon, N.1
  • 3
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • Herskowitz I: MAP kinase pathways in yeast: for mating and more. Cell 1995, 80:187-197. Recent comprehensive review of MAPK pathways in yeasts.
    • (1995) Cell , vol.80 , pp. 187-197
    • Herskowitz, I.1
  • 4
    • 0028823892 scopus 로고
    • Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast
    • Waskiewicz AJ, Cooper JA: Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast. Curr Opin Cell Biol 1995, 7:798-805. Recent overview of MAPK pathways in metazoans and yeasts.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 798-805
    • Waskiewicz, A.J.1    Cooper, J.A.2
  • 5
    • 0028331458 scopus 로고
    • NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway
    • Costigan C, Kolodrubetz D, Snyder M: NHP6A and NHP6B, which encode HMG1-like proteins, are candidates for downstream components of the yeast SLT2 mitogen-activated protein kinase pathway. Mol Cell Biol 1994, 14:2391-2403. Identification of NHP6A and NHP6B, HMG-box proteins, as targets for the MPK1 cell integrity MAPK module in S. cerevisiae. Overexpression of either protein can rescue the phenotype of an MPK1 deletion.
    • (1994) Mol Cell Biol , vol.14 , pp. 2391-2403
    • Costigan, C.1    Kolodrubetz, D.2    Snyder, M.3
  • 6
    • 0029092609 scopus 로고
    • Yeast rlm1 encodes a serum response factor-like protein that may function downstream of the mpk1 (slt2) mitogen-activated protein-kinase pathway
    • Watanabe Y, Irie K, Matsumoto K: Yeast rlm1 encodes a serum response factor-like protein that may function downstream of the mpk1 (slt2) mitogen-activated protein-kinase pathway. Mol Cell Biol 1995, 15:5740-5749. Genetic and molecular characterization of RLM1, a novel MADS-box protein, as a target for the MPK1 cell integrity MAPK module in S. cerevisiae. Demonstrates that transcriptional activation through RLM1-binding sites can rescue the phenotype of an MPK1 deletion.
    • (1995) Mol Cell Biol , vol.15 , pp. 5740-5749
    • Watanabe, Y.1    Irie, K.2    Matsumoto, K.3
  • 7
    • 0028106363 scopus 로고
    • The HOG pathway controls osmotic regulation of transcription via the stress response element (STRE) of the Saccharomyces cerevisiae CTT1 gene
    • Schuller C, Brewster JL, Alexander MR, Gustin MC, Ruis H: The HOG pathway controls osmotic regulation of transcription via the stress response element (STRE) of the Saccharomyces cerevisiae CTT1 gene. EMBO J 1994, 13:4382-4389.
    • (1994) EMBO J , vol.13 , pp. 4382-4389
    • Schuller, C.1    Brewster, J.L.2    Alexander, M.R.3    Gustin, M.C.4    Ruis, H.5
  • 8
    • 0029395010 scopus 로고
    • Stress signaling in yeast
    • Ruis H, Schuller C: Stress signaling in yeast. Bioessays 1995, 17:959-965.
    • (1995) Bioessays , vol.17 , pp. 959-965
    • Ruis, H.1    Schuller, C.2
  • 9
    • 0029585835 scopus 로고
    • Schizosccharomyces pombe atf1+ encodes a transcription factor required for sexual development and entry into stationary phase
    • Takeda T, Toda T, Kominami K, Kohnosu A, Yanagida M, Jones N: Schizosccharomyces pombe atf1+ encodes a transcription factor required for sexual development and entry into stationary phase. EMBO J 1995, 14:6193-6208.
    • (1995) EMBO J , vol.14 , pp. 6193-6208
    • Takeda, T.1    Toda, T.2    Kominami, K.3    Kohnosu, A.4    Yanagida, M.5    Jones, N.6
  • 10
    • 0028784204 scopus 로고
    • Jun cooperates with the ETS-domain protein Pointed to induce photoreceptor R7 fate in the Drosophila eye
    • Treier M, Bohmann D, Mlodzik M: Jun cooperates with the ETS-domain protein Pointed to induce photoreceptor R7 fate in the Drosophila eye. Cell 1995, 83:753-760. Use of a mutagenically activated form of human c-JUN containing acidic residues at potential phosphorylation sites to show that JUN activation can induce Drosophila R7 photoreceptor cell formation independently of activation of the Ras→Raf→ERK module. Biochemical demonstration that c-JUN and PointedP2 functionally cooperate at a composite Ets-AP-1 promoter element.
    • (1995) Cell , vol.83 , pp. 753-760
    • Treier, M.1    Bohmann, D.2    Mlodzik, M.3
  • 11
    • 0027984806 scopus 로고
    • The ETS domain protein pointed-P2 is a target of MAP kinase in the sevenless signal transduction pathway
    • Brunner D, Ducker K, Oellers N, Hafen E, Scholz H, Klambt C: The ETS domain protein pointed-P2 is a target of MAP kinase in the sevenless signal transduction pathway. Nature 1994, 370:386-389. Genetic demonstration that the ETS-domain protein PointedP2 acts downstream of the Rolled/ERKA MAPK, and that both PointedP2 and the repressor Van are targets for Rolled/ERKA in vitro.
    • (1994) Nature , vol.370 , pp. 386-389
    • Brunner, D.1    Ducker, K.2    Oellers, N.3    Hafen, E.4    Scholz, H.5    Klambt, C.6
  • 12
    • 0028239896 scopus 로고
    • The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway
    • O'Neill EM, Rebay I, Tjian R, Rubin GM: The activities of two Ets-related transcription factors required for Drosophila eye development are modulated by the Ras/MAPK pathway. Cell 1994, 78:137-147. Genetic evidence that the ETS proteins PointedP2 and Yan play opposing roles in Drosophila R7 photoreceptor cell development. Use of tissue culture assay to show that activation by PointedP2 is positively regulated, and repression by Yan negatively regulated, by direct Rolled/ERKA phosphorylation.
    • (1994) Cell , vol.78 , pp. 137-147
    • O'Neill, E.M.1    Rebay, I.2    Tjian, R.3    Rubin, G.M.4
  • 13
    • 0029019928 scopus 로고
    • Yan functions as a general inhibitor of differentiation and is negatively regulated by activation of the Ras1/MAPK pathway
    • Rebay I, Rubin GM: Yan functions as a general inhibitor of differentiation and is negatively regulated by activation of the Ras1/MAPK pathway. Cell 1995, 81:857-866. Mutation of potential Rolled MAPK sites in the Yan repressor creates a constitutively active form of the protein that cannot be regulated by the Ras→Raf→ERK module. Demonstration that MAPK phoshorylation of Yan apparently destabilizes the protein in vivo, and causes its relocalization to the cytoplasm in tissue culture cells.
    • (1995) Cell , vol.81 , pp. 857-866
    • Rebay, I.1    Rubin, G.M.2
  • 14
    • 0027930236 scopus 로고
    • Drosophila Jun mediates Ras-dependent photoreceptor determination
    • Bohmann D, Ellis MC, Staszewski LM, Mlodzik M: Drosophila Jun mediates Ras-dependent photoreceptor determination. Cell 1994, 78:973-986. Genetic study that uses dJUN derivatives that lack activation domains to demonstrate that dJUN activity is required for R7 photoreceptor cell development, and that in a genetically sensitized background, dJUN levels are limiting for R7 photoreceptor cell development.
    • (1994) Cell , vol.78 , pp. 973-986
    • Bohmann, D.1    Ellis, M.C.2    Staszewski, L.M.3    Mlodzik, M.4
  • 17
    • 0029595272 scopus 로고
    • The torso response element binds GAGA and NTF-1/ELF-1, and regulates tailless by relief of repression
    • Liaw G-J, Rudolph KM, Huang J-D, Dubnicoff T, Courey AJ, Lengyel JA: The torso response element binds GAGA and NTF-1/ELF-1, and regulates tailless by relief of repression. Genes Dev 1995, 9:3163-3176. Identification of the t-RE, a repressor element that regulates tailless expression, and genetic demonstration that its binding factor, the zinc-finger protein NTF-1, is important for its function.
    • (1995) Genes Dev , vol.9 , pp. 3163-3176
    • Liaw, G.-J.1    Rudolph, K.M.2    Huang, J.-D.3    Dubnicoff, T.4    Courey, A.J.5    Lengyel, J.A.6
  • 18
    • 0028214142 scopus 로고
    • Regulation of the Dorsal morphogen by the Toll and Torso signaling pathways: A receptor tyrosine kinase selectively masks transcriptional repression
    • Rusch J, Levine M: Regulation of the Dorsal morphogen by the Toll and Torso signaling pathways: a receptor tyrosine kinase selectively masks transcriptional repression. Genes Dev 1994, 8:1247-1257. Demonstration that the Toll and Torso signalling pathways act in combination to control activity of VREs in the Drosophila embryo.
    • (1994) Genes Dev , vol.8 , pp. 1247-1257
    • Rusch, J.1    Levine, M.2
  • 19
    • 0029592140 scopus 로고
    • Binding sites for transcription factor NTF-1/Elf-1 contribute to the ventral repression of decapentaplegic
    • Huang J-D, Dubnicoff T, Liaw G-J, Bai Y, Valentine S, Shirokawa JM, Lengyel JA, Courey AJ: Binding sites for transcription factor NTF-1/Elf-1 contribute to the ventral repression of decapentaplegic. Genes Dev 1995, 9:3177-3189. Characterization of proteins binding to the VRE in Drosophila. Demonstration that Dorsal-mediated repression involves the action of compressor elements which bind the zinc-finger protein NTF-1, which is also implicated in repression of the tailless promoter.
    • (1995) Genes Dev , vol.9 , pp. 3177-3189
    • Huang, J.-D.1    Dubnicoff, T.2    Liaw, G.-J.3    Bai, Y.4    Valentine, S.5    Shirokawa, J.M.6    Lengyel, J.A.7    Courey, A.J.8
  • 20
    • 0029951506 scopus 로고    scopus 로고
    • The pruned gene encodes the Drosophila Serum Response Factor and regulates cytoplasmic outgrowth and terminal branching of the tracheal system
    • in press
    • Guillemin K, Groppe J, Ducker K, Treisman R, Hafen E, Affolter M, Krasnow M: The pruned gene encodes the Drosophila Serum Response Factor and regulates cytoplasmic outgrowth and terminal branching of the tracheal system. Development 1996, in press. Demonstration that Pruned, the D. melanogaster SRF homologue, is required for tracheole formation, and that constitutively active human SRF is sufficient for tracheole formation in Drosophila, thus placing SRF-controlled genes downstream of the Breathless RTK.
    • (1996) Development
    • Guillemin, K.1    Groppe, J.2    Ducker, K.3    Treisman, R.4    Hafen, E.5    Affolter, M.6    Krasnow, M.7
  • 21
    • 0029585636 scopus 로고
    • The C elegans gene lin-1 encodes and ETS-domain protein and defines a branch of the vulval induction pathway
    • Beitel GJ, Tuck S, Greenwald I, Horwitz R: The C elegans gene lin-1 encodes and ETS-domain protein and defines a branch of the vulval induction pathway. Genes Dev 1995, 9:3149-3162. Identification of the ETS-domain protein LIN-1 as a negative regulator in C. elegans vulval development and a potential mediator of MAPK-stimulated transcriptional derepression.
    • (1995) Genes Dev , vol.9 , pp. 3149-3162
    • Beitel, G.J.1    Tuck, S.2    Greenwald, I.3    Horwitz, R.4
  • 22
    • 0027196007 scopus 로고
    • Lin-31, a Caenorhabditis elegans HNF-3/fork head transcription factor homolog, specifies three alternative cell fates in vulval development
    • Miller LM, Gallegos ME, Morisseau BA, Kim SK: lin-31, a Caenorhabditis elegans HNF-3/fork head transcription factor homolog, specifies three alternative cell fates in vulval development. Genes Dev 1993, 7:933-947.
    • (1993) Genes Dev , vol.7 , pp. 933-947
    • Miller, L.M.1    Gallegos, M.E.2    Morisseau, B.A.3    Kim, S.K.4
  • 24
    • 0029030855 scopus 로고
    • ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents
    • Van Dam H, Wilhelm D, Herr I, Steffen A, Herrlich P, Angel P: ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents. EMBO J 1995, 14:1798-1811. Biochemical studies that establish ATF-2 as a target of the JNK/SAPK MAPK module. Sites of phosphorylation are mapped and it is shown that the JNK/SAPKs can bind to ATF-2.
    • (1995) EMBO J , vol.14 , pp. 1798-1811
    • Van Dam, H.1    Wilhelm, D.2    Herr, I.3    Steffen, A.4    Herrlich, P.5    Angel, P.6
  • 26
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ: Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem 1995, 270:7420-7426.
    • (1995) J Biol Chem , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 27
    • 0030048767 scopus 로고    scopus 로고
    • Ras-mediated phosphorylation of a conserved threonine residue enhances the transactivation activity of c-Ets1 and c-Ets2
    • in press
    • Yang B-S, Hauser CA, Henkel G, Colman MS, Van Beveren C, Stacey KJ, Hume DA, Maki RA, Ostrowski MC: Ras-mediated phosphorylation of a conserved threonine residue enhances the transactivation activity of c-Ets1 and c-Ets2. Mol Cell Biol 1996, 16:in press. Demonstration by transfection experiments that transactivation by Ets-2 is potentiated by the Ras→Raf→ERK module via phosphorylation at T72, which lies within the region conserved in D. melanogaster PointedP2.
    • (1996) Mol Cell Biol , vol.16
    • Yang, B.-S.1    Hauser, C.A.2    Henkel, G.3    Colman, M.S.4    Van Beveren, C.5    Stacey, K.J.6    Hume, D.A.7    Maki, R.A.8    Ostrowski, M.C.9
  • 28
    • 0028670651 scopus 로고
    • Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: Mating and invasive growth
    • Roberts RL, Fink GR: Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: mating and invasive growth. Genes Dev 1994, 8:2974-2985. Characterization of the S. cerevisiae invasive growth MAPK module. Demonstration that in halpoid cells the STE12 transcription factor is required for this response, yet cannot activate FUS1, a gene that it activates in the same cells in response to mating pheromone.
    • (1994) Genes Dev , vol.8 , pp. 2974-2985
    • Roberts, R.L.1    Fink, G.R.2
  • 29
    • 0027759277 scopus 로고
    • Elements of the yeast pheromone response pathway required for filamentous growth of diploids
    • Liu H, Styles CA, Fink GR: Elements of the yeast pheromone response pathway required for filamentous growth of diploids. Science 1993, 262:1741-1744.
    • (1993) Science , vol.262 , pp. 1741-1744
    • Liu, H.1    Styles, C.A.2    Fink, G.R.3
  • 30
    • 0029005240 scopus 로고
    • Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET)
    • Price MA, Rogers AE, Treisman R: Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET). EMBO J 1995, 14:2589-2601.
    • (1995) EMBO J , vol.14 , pp. 2589-2601
    • Price, M.A.1    Rogers, A.E.2    Treisman, R.3
  • 31
    • 0028239101 scopus 로고
    • Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk2
    • Kortenjann M, Thomae O, Shaw PE: Inhibition of v-raf-dependent c-fos expression and transformation by a kinase-defective mutant of the mitogen-activated protein kinase Erk2. Mol Cell Biol 1994, 14:4815-4824.
    • (1994) Mol Cell Biol , vol.14 , pp. 4815-4824
    • Kortenjann, M.1    Thomae, O.2    Shaw, P.E.3
  • 32
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille H, Kortenjann M, Thomae O, Moomaw C, Slaughter C, Cobb MH, Shaw PE: ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J 1995, 14:951-962.
    • (1995) EMBO J , vol.14 , pp. 951-962
    • Gille, H.1    Kortenjann, M.2    Thomae, O.3    Moomaw, C.4    Slaughter, C.5    Cobb, M.H.6    Shaw, P.E.7
  • 33
    • 0028967220 scopus 로고
    • SAP1a is a nuclear target of signaling cascades involving ERKs
    • Janknecht R, Ernst WH, Nordheim A: SAP1a is a nuclear target of signaling cascades involving ERKs. Oncogene 1995, 10:1209-1216.
    • (1995) Oncogene , vol.10 , pp. 1209-1216
    • Janknecht, R.1    Ernst, W.H.2    Nordheim, A.3
  • 34
    • 0028084337 scopus 로고
    • Ternary complex factors: Growth factor regulated transcriptional activators
    • Treisman R: Ternary complex factors: growth factor regulated transcriptional activators. Curr Opin Genet Dev 1994, 4:96-101.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 96-101
    • Treisman, R.1
  • 37
    • 0029147738 scopus 로고
    • Protein-synthesis inhibitors reveal differential regulation of mitogen-activated protein-kinase and stress-activated protein-kinase pathways that converge on elk-1
    • Zinck R, Cahill MA, Kracht M, Sachsenmaier C, Hipskind RA, Nordheim A: Protein-synthesis inhibitors reveal differential regulation of mitogen-activated protein-kinase and stress-activated protein-kinase pathways that converge on elk-1. Mol Cell Biol 1995, 15:4930-4938.
    • (1995) Mol Cell Biol , vol.15 , pp. 4930-4938
    • Zinck, R.1    Cahill, M.A.2    Kracht, M.3    Sachsenmaier, C.4    Hipskind, R.A.5    Nordheim, A.6
  • 39
    • 0028144846 scopus 로고
    • c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
    • Deng T, Karin M: c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK. Nature 1994, 371:171-175. Identification of FRK, a novel Ras-dependent proline-directed kinase that phosphorylates FOS at T232, potentiating its ability to activate transcription.
    • (1994) Nature , vol.371 , pp. 171-175
    • Deng, T.1    Karin, M.2
  • 40
    • 0028631104 scopus 로고
    • Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its activation capacity
    • Bannister AJ, Brown HJ, Sutherland JA, Kouzarides T: Phosphorylation of the c-Fos and c-Jun HOB1 motif stimulates its activation capacity. Nucleic Acids Res 1994, 22:5173-5176.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5173-5176
    • Bannister, A.J.1    Brown, H.J.2    Sutherland, J.A.3    Kouzarides, T.4
  • 41
    • 0028338460 scopus 로고
    • Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Ginty DD, Bonni A, Greenberg ME: Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell 1994, 77:713-725. Identification of a novel nerve growth factor inducible, Ras-dependent protein kinase that phosphorylates CREB at Ser133. Suggests that CREB mediates responses to growth factors.
    • (1994) Cell , vol.77 , pp. 713-725
    • Ginty, D.D.1    Bonni, A.2    Greenberg, M.E.3
  • 42
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill CS, Wynne J, Treisman R: The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell 1995, 81:1159-1170. Demonstration that SRF activity can be regulated independently of its TCF partners by a signalling pathway dependent on small GTPases of the Rho family, and that SRF-linked and TCF-linked signal pathways act cooperatively at the c-fos SRE.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 43
    • 0029102041 scopus 로고
    • Structure of serum response factor core bound to DNA
    • Pellegrini L, Tan S, Richmond TJ: Structure of serum response factor core bound to DNA. Nature 1995, 376:490-498.
    • (1995) Nature , vol.376 , pp. 490-498
    • Pellegrini, L.1    Tan, S.2    Richmond, T.J.3
  • 44
    • 0029154633 scopus 로고
    • Molecular mechanisms of cell-type determination in budding yeast
    • Johnson AD: Molecular mechanisms of cell-type determination in budding yeast. Curr Opin Genet Dev 1995, 5:552-558. Useful review of combinatorial behaviour of STE12 in yeast. Note that STE12 IS present in diploid cells, however!
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 552-558
    • Johnson, A.D.1
  • 45
    • 0028641180 scopus 로고
    • ACPR, a STE12 homologue from Candida albicans, is a strong inducer of pseudohyphae in Saccharomyces cerevisiae haploids and diploids
    • Singh P, Ganesan K, Malathi K, Ghosh D, Datta A: ACPR, a STE12 homologue from Candida albicans, is a strong inducer of pseudohyphae in Saccharomyces cerevisiae haploids and diploids. Biochem Biophys Res Commun 1994, 205:1079-1085.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1079-1085
    • Singh, P.1    Ganesan, K.2    Malathi, K.3    Ghosh, D.4    Datta, A.5
  • 46
    • 0028068652 scopus 로고
    • Identification of a putative transcription factor in Candida albicans that can complement the mating defect of Saccharomyces cerevisiae ste12 mutants
    • Malathi K, Ganesan K, Datta A: Identification of a putative transcription factor in Candida albicans that can complement the mating defect of Saccharomyces cerevisiae ste12 mutants. J Biol Chem 1994, 269:22945-22951.
    • (1994) J Biol Chem , vol.269 , pp. 22945-22951
    • Malathi, K.1    Ganesan, K.2    Datta, A.3
  • 47
    • 0028569082 scopus 로고
    • Suppression of hyphal formation in Candida albicans by mutation of a STE12 homolog
    • Liu H, Kohler J, Fink GR: Suppression of hyphal formation in Candida albicans by mutation of a STE12 homolog. Science 1994, 266:1723-1726.
    • (1994) Science , vol.266 , pp. 1723-1726
    • Liu, H.1    Kohler, J.2    Fink, G.R.3
  • 48
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MPK1 kinase cascade in Saccharomyces cerevisiae
    • Nonaka H, Tanaka K, Hirano H, Fujiwara T, Kohno H, Umikawa M, Mino A, Takai Y: A downstream target of RHO1 small GTP binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MPK1 kinase cascade in Saccharomyces cerevisiae. EMBO J 1995, 14:5931-5938.
    • (1995) EMBO J , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 49
    • 0028785254 scopus 로고
    • The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation
    • Werner MH, Clore M, Fisher CL, Fisher RJ, Trinh L, Shiloach J, Gronenbom AM: The solution structure of the human ETS1-DNA complex reveals a novel mode of binding and true side chain intercalation. Cell 1995, 83:761-771.
    • (1995) Cell , vol.83 , pp. 761-771
    • Werner, M.H.1    Clore, M.2    Fisher, C.L.3    Fisher, R.J.4    Trinh, L.5    Shiloach, J.6    Gronenbom, A.M.7
  • 50
    • 0027518831 scopus 로고
    • The Drosophila gene pointed encodes two ETS-like proteins which are involved in the development of the midline glial cells
    • Klambt C: The Drosophila gene pointed encodes two ETS-like proteins which are involved in the development of the midline glial cells. Development 1993, 117:163-176.
    • (1993) Development , vol.117 , pp. 163-176
    • Klambt, C.1
  • 51
  • 52
    • 0026661584 scopus 로고
    • Control of transcription factors by signal transduction pathways: The beginning of the end
    • Karin M, Smeal T: Control of transcription factors by signal transduction pathways: the beginning of the end. Trends Biochem Sci 1992, 17:418-422.
    • (1992) Trends Biochem Sci , vol.17 , pp. 418-422
    • Karin, M.1    Smeal, T.2
  • 53
    • 0028875388 scopus 로고
    • Hemipterous encodes a novel Drosophila MAP kinase kinase, required for epithelial-cell sheet movement
    • Glise B, Bourbon H, Noselli S: Hemipterous encodes a novel Drosophila MAP kinase kinase, required for epithelial-cell sheet movement. Cell 1995, 83:451-461.
    • (1995) Cell , vol.83 , pp. 451-461
    • Glise, B.1    Bourbon, H.2    Noselli, S.3
  • 54
    • 0029156416 scopus 로고
    • Cytokines and STATs: How can signals achieve specificity?
    • Ivashkiv LB: Cytokines and STATs: how can signals achieve specificity? Immunity 1995, 3:1-4.
    • (1995) Immunity , vol.3 , pp. 1-4
    • Ivashkiv, L.B.1
  • 55
    • 0028609209 scopus 로고
    • JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation
    • Kallunki T, Su B, Tsigelny I, Sluss HK, Derijard B, Moore G, Davis R, Karin M: JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev 1994, 8:2996-3007. Investigation of the specificity of JUN phosphorylation by different JNK/SAPK isoforms. Shows that a short peptide sequence which differs between different JNK/SAPK isoforms determines the efficiency of JUN phosphorylation. Suggests that the different kinase isoforms may have slightly different specificities.
    • (1994) Genes Dev , vol.8 , pp. 2996-3007
    • Kallunki, T.1    Su, B.2    Tsigelny, I.3    Sluss, H.K.4    Derijard, B.5    Moore, G.6    Davis, R.7    Karin, M.8
  • 56
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • Hibi M, Lin A, Smeal T, Minden A, Karin M: Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes Dev 1993, 7:2135-2148.
    • (1993) Genes Dev , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 57
    • 0028061674 scopus 로고
    • Signal transduction by tumor necrosis factor mediated by JNK protein kinases
    • Sluss HK, Barrett T, Derijard B, Davis RJ: Signal transduction by tumor necrosis factor mediated by JNK protein kinases. Mol Cell Biol 1994, 14:8376-8384.
    • (1994) Mol Cell Biol , vol.14 , pp. 8376-8384
    • Sluss, H.K.1    Barrett, T.2    Derijard, B.3    Davis, R.J.4
  • 58
    • 0026635602 scopus 로고
    • Phorbol esters stimulate the phosphorylation of c-Jun but not v-Jun: Regulation by the N-terminal delta domain
    • Adler V, Franklin CC, Kraft AS: Phorbol esters stimulate the phosphorylation of c-Jun but not v-Jun: regulation by the N-terminal delta domain. Proc Natl Acad Sci USA 1992, 89:5341-5345.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5341-5345
    • Adler, V.1    Franklin, C.C.2    Kraft, A.S.3
  • 59
    • 0028902996 scopus 로고
    • Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: Implications for repression of c-Jun function
    • Dai T, Rubie E, Franklin CC, Kraft A, Gillespie DA, Avruch J, Kyriakis JM, Woodgett JR: Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: implications for repression of c-Jun function. Oncogene 1995, 10:849-855.
    • (1995) Oncogene , vol.10 , pp. 849-855
    • Dai, T.1    Rubie, E.2    Franklin, C.C.3    Kraft, A.4    Gillespie, D.A.5    Avruch, J.6    Kyriakis, J.M.7    Woodgett, J.R.8
  • 60
    • 0028245271 scopus 로고
    • A peptide encoding the c-Jun delta domain inhibits the activity of a c-jun amino-terminal protein kinase
    • Adler V, Unlap T, Kraft AS: A peptide encoding the c-Jun delta domain inhibits the activity of a c-jun amino-terminal protein kinase. J Biol Chem 1994, 269:11186-11191.
    • (1994) J Biol Chem , vol.269 , pp. 11186-11191
    • Adler, V.1    Unlap, T.2    Kraft, A.S.3
  • 62
    • 0028879263 scopus 로고
    • Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction
    • Cano E, Hazzalin CA, Kardalinou E, Buckle RS, Mahadevan LC: Neither ERK nor JNK/SAPK MAP kinase subtypes are essential for histone H3/HMG-14 phosphorylation or c-fos and c-jun induction. J Cell Sci 1995, 108:3599-3609.
    • (1995) J Cell Sci , vol.108 , pp. 3599-3609
    • Cano, E.1    Hazzalin, C.A.2    Kardalinou, E.3    Buckle, R.S.4    Mahadevan, L.C.5
  • 63
    • 0027253814 scopus 로고
    • FUS3 phosphorylates multiple components of the mating signal transduction cascade: Evidence for STE12 and FAR1
    • Elion EA, Satterberg B, Kranz JE: FUS3 phosphorylates multiple components of the mating signal transduction cascade: evidence for STE12 and FAR1. Mol Biol Cell 1993, 4:495-510.
    • (1993) Mol Biol Cell , vol.4 , pp. 495-510
    • Elion, E.A.1    Satterberg, B.2    Kranz, J.E.3
  • 64
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill CS, Treisman R: Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 1995, 80:199-211. Comprehensive overview of transcriptional regulation by extracellular signals.
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.S.1    Treisman, R.2
  • 65
    • 0029006550 scopus 로고
    • Intramolecular signal transduction in c-Jun
    • Papavassiliou AG, Treier M, Bohmann D: Intramolecular signal transduction in c-Jun. EMBO J 1995, 14:2014-2019. Generation of an activated Jun derivative by substitution of phosphoacceptors with acidic residues. Demonstration that amino-terminal phosphorylations affect the phosphorylation status of carboxy-terminal sites that affect DNA binding.
    • (1995) EMBO J , vol.14 , pp. 2014-2019
    • Papavassiliou, A.G.1    Treier, M.2    Bohmann, D.3
  • 66
    • 0028787249 scopus 로고
    • The mos/map kinase pathway stabilizes c-fos by phosphorylation and augments its transforming activity in NIH 3T3 cells
    • Okazaki K, Sagata N: The mos/map kinase pathway stabilizes c-fos by phosphorylation and augments its transforming activity in NIH 3T3 cells. EMBO J 1995, 14:5048-5059. Demonstration that phosphorylation of FOS protein in response to activation of the ERK module causes its stabilization, and that phosphorylation can be mimicked by acidic substitutions at the phosphoacceptor sites.
    • (1995) EMBO J , vol.14 , pp. 5048-5059
    • Okazaki, K.1    Sagata, N.2
  • 67
    • 0027361017 scopus 로고
    • Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
    • Chen RH, Abate C, Blenis J: Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase. Proc Natl Acad Sci USA 1993, 90:10952-10956.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10952-10956
    • Chen, R.H.1    Abate, C.2    Blenis, J.3
  • 68
    • 0025173617 scopus 로고
    • Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter
    • Ofir R, Dwarki VJ, Rashid D, Verma IM: Phosphorylation of the C terminus of Fos protein is required for transcriptional transrepression of the c-fos promoter. Nature 1990, 348:80-82.
    • (1990) Nature , vol.348 , pp. 80-82
    • Ofir, R.1    Dwarki, V.J.2    Rashid, D.3    Verma, I.M.4
  • 69
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier M, Staszewski LM, Bohmann D: Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 1994, 78:787-798.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 70
    • 0028998013 scopus 로고
    • ERK2/p42 MAP kinase stimulates both autonomous and SRF-dependent DNA binding by Elk-1
    • Sharrocks AD: ERK2/p42 MAP kinase stimulates both autonomous and SRF-dependent DNA binding by Elk-1. FEBS Lett 1995, 368:77-80.
    • (1995) FEBS Lett , vol.368 , pp. 77-80
    • Sharrocks, A.D.1
  • 71
    • 0027385031 scopus 로고
    • A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity
    • Rivera VM, Miranti CK, Misra RP, Ginty DD, Chen RH, Blenis J, Greenberg ME: A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. Mol Cell Biol 1993, 13:6260-6273.
    • (1993) Mol Cell Biol , vol.13 , pp. 6260-6273
    • Rivera, V.M.1    Miranti, C.K.2    Misra, R.P.3    Ginty, D.D.4    Chen, R.H.5    Blenis, J.6    Greenberg, M.E.7
  • 72
    • 0024362535 scopus 로고
    • Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth factor induction
    • Herrera RE, Shaw PE, Nordheim A: Occupation of the c-fos serum response element in vivo by a multi-protein complex is unaltered by growth factor induction. Nature 1989, 340:68-70.
    • (1989) Nature , vol.340 , pp. 68-70
    • Herrera, R.E.1    Shaw, P.E.2    Nordheim, A.3
  • 73
    • 0028170641 scopus 로고
    • Serum-regulated transcription by serum response factor (SRF): A novel role for the DNA binding domain
    • Hill CS, Wynne J, Treisman R: Serum-regulated transcription by serum response factor (SRF): a novel role for the DNA binding domain. EMBO J 1994, 13:5421-5432.
    • (1994) EMBO J , vol.13 , pp. 5421-5432
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 74
    • 0028048773 scopus 로고
    • Two pathways for serum regulation of the c-fos serum response element require specific sequence elements and a minimal domain of serum response factor
    • Johansen FE, Prywes R: Two pathways for serum regulation of the c-fos serum response element require specific sequence elements and a minimal domain of serum response factor. Mol Cell Biol 1994, 14:5920-5928.
    • (1994) Mol Cell Biol , vol.14 , pp. 5920-5928
    • Johansen, F.E.1    Prywes, R.2
  • 75
    • 0027261515 scopus 로고
    • Down-regulation of the Drosophila morphogen Bicoid by the torso receptor-mediated signal transduction cascade
    • Ronchi E, Treisman J, Dostatni N, Struhl G, Desplan C: Down-regulation of the Drosophila morphogen Bicoid by the torso receptor-mediated signal transduction cascade. Cell 1993, 74:347-355.
    • (1993) Cell , vol.74 , pp. 347-355
    • Ronchi, E.1    Treisman, J.2    Dostatni, N.3    Struhl, G.4    Desplan, C.5
  • 79
    • 0027965563 scopus 로고
    • Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors
    • Hipskind RA, Buscher D, Nordheim A, Baccarini M: Ras/MAP kinase-dependent and -independent signaling pathways target distinct ternary complex factors. Genes Dev 1994, 8:1803-1816.
    • (1994) Genes Dev , vol.8 , pp. 1803-1816
    • Hipskind, R.A.1    Buscher, D.2    Nordheim, A.3    Baccarini, M.4
  • 80
    • 0029118202 scopus 로고
    • Pheromone signaling in Saccharomyces cerevisiae requires the small GTP-binding protein cdc42p and its activator cdc24
    • Zhao ZS, Leung T, Manser E, Lim L: Pheromone signaling in Saccharomyces cerevisiae requires the small GTP-binding protein cdc42p and its activator cdc24. Mol Cell Biol 1995, 15:5246-5257.
    • (1995) Mol Cell Biol , vol.15 , pp. 5246-5257
    • Zhao, Z.S.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 81
    • 0029157469 scopus 로고
    • Role for the rho-family GTPase cdc42 in yeast mating-pheromone signal pathway
    • Simon MN, De Virgilio C, Souza B, Pringle JR, Abo A, Reed SI: Role for the rho-family GTPase cdc42 in yeast mating-pheromone signal pathway. Nature 1995, 376:702-705.
    • (1995) Nature , vol.376 , pp. 702-705
    • Simon, M.N.1    De Virgilio, C.2    Souza, B.3    Pringle, J.R.4    Abo, A.5    Reed, S.I.6
  • 82
    • 0029028962 scopus 로고
    • Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor
    • Maeda T, Takekawa M, Saito H: Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 1995, 269:554-558.
    • (1995) Science , vol.269 , pp. 554-558
    • Maeda, T.1    Takekawa, M.2    Saito, H.3
  • 83
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • Derijard B, Hibi M, Wu IH, Barrett T, Su B, Deng T, Karin M, Davis RJ: JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 1994, 76:1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 84
    • 0028820587 scopus 로고
    • Rho-family GTPases regulate p38 mitogen-activated protein-kinase through the downstream mediator pak1
    • Zhang SJ, Han JH, Sells MA, Chernoff J, Knaus UG, Ulevitch RJ, Bokoch GM: Rho-family GTPases regulate p38 mitogen-activated protein-kinase through the downstream mediator pak1. J Biol Chem 1995, 270:23934-23936.
    • (1995) J Biol Chem , vol.270 , pp. 23934-23936
    • Zhang, S.J.1    Han, J.H.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 86
    • 0029101360 scopus 로고
    • An essential role for rho, rac, and cdc42 GTPases in cell-cycle progression through G1
    • Olson MF, Ashworth A, Hall A: An essential role for rho, rac, and cdc42 GTPases in cell-cycle progression through G1. Science 1995, 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 87
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden A, Lin A, Claret FX, Abo A, Karin M: Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 1995, 81:1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 88
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu JC, Teramoto H, Crespo P, Xu N, Miki T, Gutkind JS: The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 1995, 81:1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 91
    • 0025296684 scopus 로고
    • Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells
    • Gaire M, Chatton B, Kedinger C: Isolation and characterization of two novel, closely related ATF cDNA clones from HeLa cells. Nucleic Acids Res 1990, 18:3467-3473.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3467-3473
    • Gaire, M.1    Chatton, B.2    Kedinger, C.3
  • 92
    • 0028329225 scopus 로고
    • MCM1 point mutants deficient in expression of alpha-specific genes: Residues important for interaction with alpha 1
    • Bruhn L, Sprague GF Jr: MCM1 point mutants deficient in expression of alpha-specific genes: residues important for interaction with alpha 1. Mol Cell Biol 1994, 14:2534-2544.
    • (1994) Mol Cell Biol , vol.14 , pp. 2534-2544
    • Bruhn, L.1    Sprague G.F., Jr.2
  • 93
    • 0027209343 scopus 로고
    • Coupling of cell identity to signal response in yeast: Interaction between the alpha 1 and STE12 proteins
    • Yuan YO, Stroke IL, Fields S: Coupling of cell identity to signal response in yeast: interaction between the alpha 1 and STE12 proteins. Genes Dev 1993, 7:1584-1597.
    • (1993) Genes Dev , vol.7 , pp. 1584-1597
    • Yuan, Y.O.1    Stroke, I.L.2    Fields, S.3
  • 94
    • 0028116591 scopus 로고
    • A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes encoding ribosomal proteins and six putative new genes, one of which encodes a putative transcriptional factor
    • Demolis N, Mallet L, Jacquet M: A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes encoding ribosomal proteins and six putative new genes, one of which encodes a putative transcriptional factor. Yeast 1994, 10:1511-1525.
    • (1994) Yeast , vol.10 , pp. 1511-1525
    • Demolis, N.1    Mallet, L.2    Jacquet, M.3
  • 95
    • 0027932666 scopus 로고
    • Yap1p, a yeast transcriptional activator that mediates multidrug resistance, regulates the metabolic stress response
    • Gounalaki N, Thireos G: Yap1p, a yeast transcriptional activator that mediates multidrug resistance, regulates the metabolic stress response. EMBO J 1994, 13:4036-4041.
    • (1994) EMBO J , vol.13 , pp. 4036-4041
    • Gounalaki, N.1    Thireos, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.