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Volumn 22, Issue 20, 2002, Pages 7105-7119

The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting its localization in Schizosaccharomyces pombe

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE; NITROGEN; PROTEIN 14 3 3;

EID: 0036786954     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.22.20.7105-7119.2002     Document Type: Article
Times cited : (55)

References (75)
  • 1
    • 0028903288 scopus 로고
    • 14-3-3 Proteins on the MAP
    • Aitken, A. 1995. 14-3-3 proteins on the MAP. Trends Biochem. Sci. 20:95-97.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 95-97
    • Aitken, A.1
  • 2
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 And its possible role in co-ordinating multiple signaling pathways
    • Aitken, A. 1996. 14-3-3 and its possible role in co-ordinating multiple signaling pathways. Trends Cell Biol. 6:341-347.
    • (1996) Trends Cell Biol. , vol.6 , pp. 341-347
    • Aitken, A.1
  • 4
    • 0031899619 scopus 로고    scopus 로고
    • Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast
    • Andoh, T., T. J. Kato, Y. Matsui, and A. Toh-e. 1998. Phosphoinositide-specific phospholipase C forms a complex with 14-3-3 proteins and is involved in expression of UV resistance in fission yeast. Mol. Gen. Genet. 258:139-147.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 139-147
    • Andoh, T.1    Kato, T.J.2    Matsui, Y.3    Toh-e, A.4
  • 5
    • 0029833462 scopus 로고    scopus 로고
    • Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe
    • Barr, M. M., H. Tu, L. Van Aelst, and M. Wigler. 1996. Identification of Ste4 as a potential regulator of Byr2 in the sexual response pathway of Schizosaccharomyces pombe. Mol. Cell. Biol. 16:5597-5603.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5597-5603
    • Barr, M.M.1    Tu, H.2    Van Aelst, L.3    Wigler, M.4
  • 6
    • 0032539775 scopus 로고    scopus 로고
    • The Byr2 kinase translocates to the plasma membrane in a Ras1-dependent manner
    • Bauman, P., Q. Cheng, and C. F. Albright. 1998. The Byr2 kinase translocates to the plasma membrane in a Ras1-dependent manner. Biochem. Biophys. Res. Commun. 244:468-474.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 468-474
    • Bauman, P.1    Cheng, Q.2    Albright, C.F.3
  • 7
    • 0029166558 scopus 로고
    • BCR and RAF form a complex in vivo via 14-3-3 proteins
    • Braselmann, S., and F. McCormick. 1995. BCR and RAF form a complex in vivo via 14-3-3 proteins. EMBO J. 14:4839-4848.
    • (1995) EMBO J. , vol.14 , pp. 4839-4848
    • Braselmann, S.1    McCormick, F.2
  • 8
    • 0030999664 scopus 로고    scopus 로고
    • 14-3-3ε positively regulates Rasmediated signaling in Drosophila
    • Chang, H. C., and G. M. Rubin. 1997. 14-3-3ε positively regulates Rasmediated signaling in Drosophila. Genes Dev. 11:1132-1139.
    • (1997) Genes Dev. , vol.11 , pp. 1132-1139
    • Chang, H.C.1    Rubin, G.M.2
  • 9
    • 0033558882 scopus 로고    scopus 로고
    • Association of Chk1 with 14-3-3 proteins is stimulated by DNA damage
    • Chen, L., T.-H. Liu, and N. C. Walworth. 1999. Association of Chk1 with 14-3-3 proteins is stimulated by DNA damage. Genes Dev. 13:675-685.
    • (1999) Genes Dev. , vol.13 , pp. 675-685
    • Chen, L.1    Liu, T.-H.2    Walworth, N.C.3
  • 11
    • 0032974109 scopus 로고    scopus 로고
    • Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site
    • Dalal, S., C. Schweitzer, J. Gan, and J. DeCaprio. 1999. Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site. Mol. Cell. Biol. 19:4465-4479.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4465-4479
    • Dalal, S.1    Schweitzer, C.2    Gan, J.3    DeCaprio, J.4
  • 12
    • 0032412564 scopus 로고    scopus 로고
    • Fusion of a fission yeast
    • Davey, J. 1998. Fusion of a fission yeast. Yeast 14:1529-1566.
    • (1998) Yeast , vol.14 , pp. 1529-1566
    • Davey, J.1
  • 13
    • 0031968587 scopus 로고    scopus 로고
    • Oscillatory nuclear movement in fission yeast meiotic prophase is driven by astral microtubules as revealed by continuous observation of chromosomes and microtubules in living cells
    • Ding, D.-Q., Y. Chikashige, T. Haraguchi, and Y. Hiraoka. 1998. Oscillatory nuclear movement in fission yeast meiotic prophase is driven by astral microtubules as revealed by continuous observation of chromosomes and microtubules in living cells. J. Cell Sci. 111:701-712.
    • (1998) J. Cell Sci. , vol.111 , pp. 701-712
    • Ding, D.-Q.1    Chikashige, Y.2    Haraguchi, T.3    Hiraoka, Y.4
  • 16
    • 0030950042 scopus 로고    scopus 로고
    • General purpose tagging vectors for fission yeast
    • Forsburg, S. L., and D. A. Sherman. 1997. General purpose tagging vectors for fission yeast. Gene 191:191-195.
    • (1997) Gene , vol.191 , pp. 191-195
    • Forsburg, S.L.1    Sherman, D.A.2
  • 17
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed, E., M. Symons, S. G. Macdonald, F. McCormick, and R. Ruggieri. 1994. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 265:1713-1716.
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    Macdonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 19
    • 0022554044 scopus 로고
    • Role of a Ras homolog in the life cycle of Schizosaccharomyces pombe
    • Fukui, Y., T. Kozasa, Y. Kaziro, T. Takeda, and M. Yamamoto. 1986. Role of a Ras homolog in the life cycle of Schizosaccharomyces pombe. Cell 44:329-336.
    • (1986) Cell , vol.44 , pp. 329-336
    • Fukui, Y.1    Kozasa, T.2    Kaziro, Y.3    Takeda, T.4    Yamamoto, M.5
  • 22
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: a laboratory manual
    • Harlow, E.1    Lane, D.2
  • 23
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie, K., Y. Gotoh, B. M. Yashar, B. Errede, E. Nishida, and K. Matsumoto. 1994. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 265:1716-1719.
    • (1994) Science , vol.265 , pp. 1716-1719
    • Irie, K.1    Gotoh, Y.2    Yashar, B.M.3    Errede, B.4    Nishida, E.5    Matsumoto, K.6
  • 25
    • 0030174310 scopus 로고    scopus 로고
    • Genetic analysis of the sam mutations, which induce sexual development with no requirement for nutritional starvation in fission yeast
    • Katayama, S., F. Ozoe, R. Kurokawa, K. Tanaka, T. Nakagawa, H. Matsuda, and M. Kawamukai. 1996. Genetic analysis of the sam mutations, which induce sexual development with no requirement for nutritional starvation in fission yeast. Biosci. Biotechnol. Biochem. 60:994-999.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 994-999
    • Katayama, S.1    Ozoe, F.2    Kurokawa, R.3    Tanaka, K.4    Nakagawa, T.5    Matsuda, H.6    Kawamukai, M.7
  • 26
    • 0027058053 scopus 로고
    • Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe
    • Kawamukai, M., J. Gerst, J. Field, M. Riggs, L. Rodgers, M. Wigler, and D. Young. 1992. Genetic and biochemical analysis of the adenylyl cyclase-associated protein, cap, in Schizosaccharomyces pombe. Mol. Biol. Cell 3:167-180.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 167-180
    • Kawamukai, M.1    Gerst, J.2    Field, J.3    Riggs, M.4    Rodgers, L.5    Wigler, M.6    Young, D.7
  • 27
    • 0033000999 scopus 로고    scopus 로고
    • Isolation of a novel gene, moc2, encoding a putative RNA helicase as a suppressor of sterile strains in Schizosaccharomyces pombe
    • Kawamukai, M. 1999. Isolation of a novel gene, moc2, encoding a putative RNA helicase as a suppressor of sterile strains in Schizosaccharomyces pombe. Biochim. Biophys. Acta 1446:93-101.
    • (1999) Biochim. Biophys. Acta , vol.1446 , pp. 93-101
    • Kawamukai, M.1
  • 28
    • 0028269495 scopus 로고
    • Efficient targeted integration at leul-32 and ura4-294 in Schizosaccharomyces pombe
    • Keeney, J. B., and J. D. Boeke. 1994. Efficient targeted integration at leul-32 and ura4-294 in Schizosaccharomyces pombe. Genetics 136:849-856.
    • (1994) Genetics , vol.136 , pp. 849-856
    • Keeney, J.B.1    Boeke, J.D.2
  • 29
    • 0025943077 scopus 로고
    • The Schizosaccharomyces pombe mam2 gene encodes a putative pheromone receptor which has a significant homology with the Saccharomyces cerevisiae Ste2 protein
    • Kitamura, K., and C. Shimoda. 1991. The Schizosaccharomyces pombe mam2 gene encodes a putative pheromone receptor which has a significant homology with the Saccharomyces cerevisiae Ste2 protein. EMBO J. 10:3743-3751.
    • (1991) EMBO J. , vol.10 , pp. 3743-3751
    • Kitamura, K.1    Shimoda, C.2
  • 30
    • 0035462049 scopus 로고    scopus 로고
    • Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual differentiation via ubiquitin proteolysis and 14-3-3 protein in fission yeast
    • Kitamura, K., S. Katayama, S. Dhut, M. Sato, Y. Watanabe, M. Yamamoto, and T. Toda. 2001. Phosphorylation of Mei2 and Ste11 by Pat1 kinase inhibits sexual differentiation via ubiquitin proteolysis and 14-3-3 protein in fission yeast. Dev. Cell 1:389-399.
    • (2001) Dev. Cell , vol.1 , pp. 389-399
    • Kitamura, K.1    Katayama, S.2    Dhut, S.3    Sato, M.4    Watanabe, Y.5    Yamamoto, M.6    Toda, T.7
  • 31
    • 0030953744 scopus 로고    scopus 로고
    • Requirement for Drosophila 14-3-3ζ in Raf-dependent photoreceptor development
    • Koekel, L., G. Vorbruggen, H. Jackle, M. Mlodzik, and D. Bohmann. 1997. Requirement for Drosophila 14-3-3ζ in Raf-dependent photoreceptor development. Genes Dev. 11:1140-1147.
    • (1997) Genes Dev. , vol.11 , pp. 1140-1147
    • Koekel, L.1    Vorbruggen, G.2    Jackle, H.3    Mlodzik, M.4    Bohmann, D.5
  • 32
    • 0033134794 scopus 로고    scopus 로고
    • Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25
    • Kumagai, A., and W. G. Dunphy. 1999. Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25. Genes Dev. 13:1067-1072.
    • (1999) Genes Dev. , vol.13 , pp. 1067-1072
    • Kumagai, A.1    Dunphy, W.G.2
  • 33
    • 0030054354 scopus 로고    scopus 로고
    • Interaction of Cdc2 and Cdc18 with a fission yeast ORC2-like protein
    • Leatherwood, J., A. Lopez-Girona, and P. Russell. 1996. Interaction of Cdc2 and Cdc18 with a fission yeast ORC2-like protein. Nature 379:360-363.
    • (1996) Nature , vol.379 , pp. 360-363
    • Leatherwood, J.1    Lopez-Girona, A.2    Russell, P.3
  • 35
    • 0033552943 scopus 로고    scopus 로고
    • Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein
    • Lopez-Girona, A., B. Furnari, O. Mondesert, and P. Russell. 1999. Nuclear localization of Cdc25 is regulated by DNA damage and a 14-3-3 protein. Nature 397:172-175.
    • (1999) Nature , vol.397 , pp. 172-175
    • Lopez-Girona, A.1    Furnari, B.2    Mondesert, O.3    Russell, P.4
  • 37
    • 0025298571 scopus 로고
    • nmt1 of fission yeast. A highly transcribed gene completely repressed by thiamine
    • Maundrell, K. 1990. nmt1 of fission yeast. A highly transcribed gene completely repressed by thiamine. J. Biol. Chem. 265:10857-10864.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10857-10864
    • Maundrell, K.1
  • 38
    • 0026025891 scopus 로고
    • Molecular genetics of fission yeast Schizosaccharomyces pombe
    • Moreno, S., A. Klar, and P. Nurse. 1991. Molecular genetics of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:795-823.
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 39
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison, D. K., G. Heidecker, U. R. Rapp, and T. D. Copeland. 1993. Identification of the major phosphorylation sites of the Raf-1 kinase. J. Biol. Chem. 268:17309-17316.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17309-17316
    • Morrison, D.K.1    Heidecker, G.2    Rapp, U.R.3    Copeland, T.D.4
  • 40
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., J. W. Tanner, P. M. Allen, and A. S. Shaw. 1996. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 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
  • 41
    • 0030853995 scopus 로고    scopus 로고
    • Use of green fluorescent protein for intracellular protein localization in living fission yeast
    • Nabeshima, K., S. Saitoh, and M. Yanagida. 1997. Use of green fluorescent protein for intracellular protein localization in living fission yeast. Methods Enzymol. 283:459-471.
    • (1997) Methods Enzymol. , vol.283 , pp. 459-471
    • Nabeshima, K.1    Saitoh, S.2    Yanagida, M.3
  • 42
    • 0023991154 scopus 로고
    • A gene which encodes a predicted protein kinase can restore some functions of the ras gene in fission yeast
    • Nadin-Davis, S. A., and A. Nasim. 1988. A gene which encodes a predicted protein kinase can restore some functions of the ras gene in fission yeast. EMBO J. 7:985-993.
    • (1988) EMBO J. , vol.7 , pp. 985-993
    • Nadin-Davis, S.A.1    Nasim, A.2
  • 43
    • 0027502790 scopus 로고
    • Functional homology of protein kinases required for sexual differentiation in Schizosaccharomyces pombe and Saccharomyces cerevisiae suggests a conserved signal transduction module in eukaryotic organisms
    • Neiman, A. M., B. J. Stevenson, H.-P. Xu, G. F. J. Sprague, 1. Herskowitz, M. Wigler, and S. Marcus. 1993. Functional homology of protein kinases required for sexual differentiation in Schizosaccharomyces pombe and Saccharomyces cerevisiae suggests a conserved signal transduction module in eukaryotic organisms. Mol. Biol. Cell 4:102-107.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 102-107
    • Neiman, A.M.1    Stevenson, B.J.2    Xu, H.-P.3    Sprague, G.F.J.4    Herskowitz, I.5    Wigler, M.6    Marcus, S.7
  • 44
    • 0025999133 scopus 로고
    • Isolation and characterization of a gene encoding a G-protein a subunit from Schizosaccharomyces pombe: Involvement in mating and sporulation pathways
    • Obara, T., M. Nakafuku, M. Yamamoto, and Y. Kaziro. 1991. Isolation and characterization of a gene encoding a G-protein a subunit from Schizosaccharomyces pombe: involvement in mating and sporulation pathways. Proc. Natl. Acad. Sci. USA 88:5877-5881.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5877-5881
    • Obara, T.1    Nakafuku, M.2    Yamamoto, M.3    Kaziro, Y.4
  • 45
    • 0026345125 scopus 로고
    • + gene, essential for sexual differentiation of Schizosaccharomyces pombe, encodes a protein with a leucine zipper motif
    • + gene, essential for sexual differentiation of Schizosaccharomyces pombe, encodes a protein with a leucine zipper motif. Nucleic Acids Res. 19:7043-7047.
    • (1991) Nucleic Acids Res , vol.19 , pp. 7043-7047
    • Okazaki, N.1    Okazaki, K.2    Tanaka, K.3    Okayama, H.4
  • 46
    • 0028879613 scopus 로고
    • Fission yeast pak1 encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating
    • Ottilie, S., P. J. Miller, D. I. Johnson, C. L. Creasy, M. A. Sells, S. Bagrodia, S. L. Forsburg, and J. Chernoff. 1995. Fission yeast pak1 encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating. EMBO J. 14:5908-5919.
    • (1995) EMBO J. , vol.14 , pp. 5908-5919
    • Ottilie, S.1    Miller, P.J.2    Johnson, D.I.3    Creasy, C.L.4    Sells, M.A.5    Bagrodia, S.6    Forsburg, S.L.7    Chernoff, J.8
  • 48
    • 0032568665 scopus 로고    scopus 로고
    • 14-3-3ζ binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove
    • Petosa, C., S. C. Masters, L. A. Bankston, J. Pohl, B. Wang, H. Fu, and R. C. Liddington. 1998. 14-3-3ζ 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
  • 49
    • 0031587849 scopus 로고    scopus 로고
    • 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae
    • Roberts, R. L., H.-U. Mosch, and G. R. Fink. 1997. 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Cell 89:1055-1065.
    • (1997) Cell , vol.89 , pp. 1055-1065
    • Roberts, R.L.1    Mosch, H.-U.2    Fink, G.R.3
  • 51
    • 0030853961 scopus 로고    scopus 로고
    • Negative regulation of Raf activity by binding of 14-3-3 to the amino terminus of Raf in vivo
    • Rommel, C., G. Radziwill, K. Moelling, and E. Hafen. 1997. Negative regulation of Raf activity by binding of 14-3-3 to the amino terminus of Raf in vivo. Mech. Dev. 64:95-104.
    • (1997) Mech. Dev. , vol.64 , pp. 95-104
    • Rommel, C.1    Radziwill, G.2    Moelling, K.3    Hafen, E.4
  • 54
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
    • Sanchez, Y., C. Wong, R. S. Thoma, R. Richman, Z. Wu, H. Piwnica-Worms, and S. J. Elledge. 1997. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. Science 277:1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1    Wong, C.2    Thoma, R.S.3    Richman, R.4    Wu, Z.5    Piwnica-Worms, H.6    Elledge, S.J.7
  • 55
    • 0037154008 scopus 로고    scopus 로고
    • 14-3-3 protein interferes with the binding of RNA to the phosphorylated form of fission yeast meiotic regulator mei2p
    • Sato, M., Y. Watanabe, Y. Akiyoshi, and M. Yamamoto. 2002. 14-3-3 protein interferes with the binding of RNA to the phosphorylated form of fission yeast meiotic regulator mei2p. Curr. Biol. 12:141-145.
    • (2002) Curr. Biol. , vol.12 , pp. 141-145
    • Sato, M.1    Watanabe, Y.2    Akiyoshi, Y.3    Yamamoto, M.4
  • 56
    • 0026038558 scopus 로고
    • + encodes a transcription factor with an HMG motif that is a critical regulator of sexual development
    • + encodes a transcription factor with an HMG motif that is a critical regulator of sexual development. Genes Dev. 5:1990-1999.
    • (1991) Genes Dev. , vol.5 , pp. 1990-1999
    • Sugimoto, A.1    Iino, Y.2    Maeda, T.3    Watanabe, Y.4    Yamamoto, M.5
  • 57
    • 0027097142 scopus 로고
    • A low copy number central sequence with strict symmetry and unusual chromatin structure in fission yeast centromere
    • Takahashi, K., S. Murakami, Y. Chikashige, H. Funabiki, O. Niwa, and M. Yanagida. 1992. A low copy number central sequence with strict symmetry and unusual chromatin structure in fission yeast centromere. Mol. Biol. Cell 3:819-835.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 819-835
    • Takahashi, K.1    Murakami, S.2    Chikashige, Y.3    Funabiki, H.4    Niwa, O.5    Yanagida, M.6
  • 58
    • 0033508431 scopus 로고    scopus 로고
    • Characterization of a fission yeast SUMO-1 homologue, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation
    • Tanaka, K., J. Nishide, K. Okazaki, H. Kato, O. Niwa, T. Nakagawa, H. Matsuda, M. Kawamukai, and Y. Murakami. 1999. Characterization of a fission yeast SUMO-1 homologue, Pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation. Mol. Cell. Biol. 19:8660-8672.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8660-8672
    • Tanaka, K.1    Nishide, J.2    Okazaki, K.3    Kato, H.4    Niwa, O.5    Nakagawa, T.6    Matsuda, H.7    Kawamukai, M.8    Murakami, Y.9
  • 59
    • 0034724650 scopus 로고    scopus 로고
    • Rad24 is essential for proliferation of diploid cells in fission yeast
    • Tanaka, Y., D. Okuzaki, N. Yabuta, T. Yoneki, and H. Nojima. 2000. Rad24 is essential for proliferation of diploid cells in fission yeast. FEBS Lett. 472:254-258.
    • (2000) FEBS Lett. , vol.472 , pp. 254-258
    • Tanaka, Y.1    Okuzaki, D.2    Yabuta, N.3    Yoneki, T.4    Nojima, H.5
  • 61
    • 0025977196 scopus 로고
    • Fission yeast genes that confer resistance to staurosporine encode an AP-1-like transcription factor and a protein kinase related to the mammalian ERK1/MAP2 and budding yeast FUS3 and KSS1 kinases
    • Toda, T., M. Shimanuki, and M. Yanagida. 1991. Fission yeast genes that confer resistance to staurosporine encode an AP-1-like transcription factor and a protein kinase related to the mammalian ERK1/MAP2 and budding yeast FUS3 and KSS1 kinases. Genes Dev. 5:60-73.
    • (1991) Genes Dev. , vol.5 , pp. 60-73
    • Toda, T.1    Shimanuki, M.2    Yanagida, M.3
  • 62
    • 0030763928 scopus 로고    scopus 로고
    • Mutiple regulatory domains on the Byr2 protein kinase
    • Tu, H., M. Barr, D. L. Dong, and M. Wigler. 1997. Mutiple regulatory domains on the Byr2 protein kinase Mol. Cell. Biol. 17:5876-5887.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5876-5887
    • Tu, H.1    Barr, M.2    Dong, D.L.3    Wigler, M.4
  • 63
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion, G., Z. Luo, and J. Avruch. 1998. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394:88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 64
    • 0025806672 scopus 로고
    • byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype
    • Wang, Y., H. P. Xu, M. Riggs, L. Rodgers, and M. Wigler. 1991. byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype. Mol. Cell. Biol. 11:3554-3563.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3554-3563
    • Wang, Y.1    Xu, H.P.2    Riggs, M.3    Rodgers, L.4    Wigler, M.5
  • 65
    • 0032568944 scopus 로고    scopus 로고
    • Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3ζ disrupt its interaction with Raf-1 kinase
    • Wang, H., L. Zhang, R. Liddington, and H. Fu. 1998. Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3ζ disrupt its interaction with Raf-1 kinase. J. Biol. Chem. 273:16297-16304.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16297-16304
    • Wang, H.1    Zhang, L.2    Liddington, R.3    Fu, H.4
  • 66
    • 0028979375 scopus 로고
    • Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways
    • Xiao, B., S. J. Smerdon, D. H. Jones, G. G. Dodson, Y. Soneji, A. Aitken, and S. J. Gamblin. 1995. Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways. Nature 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
  • 67
    • 0027953513 scopus 로고
    • Concerted action of RAS and G proteins in the sexual response pathways of Schizosaccharomyces pombe
    • Xu, H.-P., M. White, S. Marcus, and M. Wigler. 1994. Concerted action of RAS and G proteins in the sexual response pathways of Schizosaccharomyces pombe. Mol. Cell. Biol. 14:50-58.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 50-58
    • Xu, H.-P.1    White, M.2    Marcus, S.3    Wigler, M.4
  • 69
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • Yaffe, M. B., and A. E. Ella. 2001. Phosphoserine/threonine-binding domains. Curr. Opin. Cell Biol. 13:131-138.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Ella, A.E.2
  • 70
    • 0001136727 scopus 로고    scopus 로고
    • Mating and sporulation in Schizosaccharomycespombe
    • J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), Cold Spring Harbor Laboratory. Press, Cold Spring Harbor, N.Y.
    • Yamamoto, M., Y. Imai, and Y. Watanabe. 1997. Mating and sporulation in Schizosaccharomycespombe, p. 1037-1106. In J. R. Pringle, J. R. Broach, and E. W. Jones (ed.), The molecular and cellular biology of the yeast saccharomyces, vol. 3. Cold Spring Harbor Laboratory. Press, Cold Spring Harbor, N.Y.
    • (1997) The molecular and cellular biology of the yeast saccharomyces , vol.3 , pp. 1037-1106
    • Yamamoto, M.1    Imai, Y.2    Watanabe, Y.3
  • 71
    • 0033561439 scopus 로고    scopus 로고
    • 2 arrest in the Xenopus oocyte: A role for 14-3-3-mediated inhibition of Cdc25 nuclear import
    • 2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import. EMBO J. 18:2174-2183.
    • (1999) EMBO J. , vol.18 , pp. 2174-2183
    • Yang, J.1    Winkler, K.2    Yoshida, M.3    Kornbluth, S.4
  • 72
    • 0032190082 scopus 로고    scopus 로고
    • Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1
    • Zeng, Y., K. Forbes, Z. Wu, S. Moreno, H. Piwnica-Worms, and T. Enoch. 1998. Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1. Nature 395:507-510.
    • (1998) Nature , vol.395 , pp. 507-510
    • Zeng, Y.1    Forbes, K.2    Wu, Z.3    Moreno, S.4    Piwnica-Worms, H.5    Enoch, T.6
  • 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 H. Piwnica-Worms. 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
    • 0028329630 scopus 로고
    • Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues
    • Zheng, C.-F., and K.-L. Guan. 1994. Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J. 13:1123-1131.
    • (1994) EMBO J. , vol.13 , pp. 1123-1131
    • Zheng, C.-F.1    Guan, K.-L.2
  • 75
    • 0033628573 scopus 로고    scopus 로고
    • Identification of a 14-3-3 homologue from Lentinus edodes as CAP (adenylyl cyclase-associated protein) interacting protein and its conservation in fission yeast
    • Zhou, G.-L., T. Yamamoto, F. Ozoe, D. Yano, K. Tanaka, H. Matsuda, and M. Kawamukai. 2000. Identification of a 14-3-3 homologue from Lentinus edodes as CAP (adenylyl cyclase-associated protein) interacting protein and its conservation in fission yeast. Biosci. Biotechnol. Biochem. 64:149-159.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 149-159
    • Zhou, G.-L.1    Yamamoto, T.2    Ozoe, F.3    Yano, D.4    Tanaka, K.5    Matsuda, H.6    Kawamukai, M.7


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