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Volumn 247, Issue 2, 1997, Pages 703-708

Dimerization of Cdc25p, the guanine-nucleotide exchange factor for ras from Saccharomyces cerevisiae, and its interaction with Sdc25p

Author keywords

Cellular signalization; Guanine exchange factor; Ras protein; Two hybrid system

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR;

EID: 0030855008     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00703.x     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0022666379 scopus 로고
    • Characterization, cloning and sequence analysis of the CDC25 gene which controls the cyclic AMP level of Saccharomyces cerevisiae
    • Camonis, J. H., Kalékine, M., Gondré, B., Garreau, H., Boy-Marcotte, E. & Jacquet, M. (1986) Characterization, cloning and sequence analysis of the CDC25 gene which controls the cyclic AMP level of Saccharomyces cerevisiae, EMBO J. 5, 375-380.
    • (1986) EMBO J. , vol.5 , pp. 375-380
    • Camonis, J.H.1    Kalékine, M.2    Gondré, B.3    Garreau, H.4    Boy-Marcotte, E.5    Jacquet, M.6
  • 2
    • 0000880266 scopus 로고
    • Molecular cloning and transcriptional analysis of the start gene CDC25 of Saccharomyces cerevisiae
    • Martegani, E., Baroni, M. D., Frascotti, G. & Alberghina, L. (1986) Molecular cloning and transcriptional analysis of the start gene CDC25 of Saccharomyces cerevisiae: EMBO J. 5, 2363-2369.
    • (1986) EMBO J. , vol.5 , pp. 2363-2369
    • Martegani, E.1    Baroni, M.D.2    Frascotti, G.3    Alberghina, L.4
  • 4
    • 0029881888 scopus 로고    scopus 로고
    • SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation
    • Boy-Marcotte, E., Ikonomi, P. & Jacquet, M. (1996) SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation, Mol. Biol. Cell 7, 529-539.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 529-539
    • Boy-Marcotte, E.1    Ikonomi, P.2    Jacquet, M.3
  • 5
    • 0026057814 scopus 로고
    • SDC25, a CDC25 like gene, which contains a RAS-activating domain is a dispensable gene of Saccharomyces cerevisiae
    • Damak, F., Boy-Marcotte, E., Le-Roscouet, D., Guilbaud, R. & Jacquet, M. (1991) SDC25, a CDC25 like gene, which contains a RAS-activating domain is a dispensable gene of Saccharomyces cerevisiae, Mol. Cell. Biol. 11, 202-212.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 202-212
    • Damak, F.1    Boy-Marcotte, E.2    Le-Roscouet, D.3    Guilbaud, R.4    Jacquet, M.5
  • 6
    • 0024602535 scopus 로고
    • The C-terminal part of a gene partially homologous to CDC25 gene suppresses the cdc25-5 mutation in Saccharomyces cerevisiae
    • Boy-Marcotte, E., Damak, F., Camonis, J., Garreau, H. & Jacquet, M. (1989) The C-terminal part of a gene partially homologous to CDC25 gene suppresses the cdc25-5 mutation in Saccharomyces cerevisiae, Gene 77, 21-30.
    • (1989) Gene , vol.77 , pp. 21-30
    • Boy-Marcotte, E.1    Damak, F.2    Camonis, J.3    Garreau, H.4    Jacquet, M.5
  • 7
    • 0027931640 scopus 로고
    • Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
    • Aronheim, A., Engelberg, D., Li, N., Al-alawi, N., Schlessinger, J. & Karin, M. (1994) Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway. Cell 78, 949-961.
    • (1994) Cell , vol.78 , pp. 949-961
    • Aronheim, A.1    Engelberg, D.2    Li, N.3    Al-alawi, N.4    Schlessinger, J.5    Karin, M.6
  • 8
    • 0027365376 scopus 로고
    • A murine CDC25/ras-GRF-related protein implicated in Ras regulation
    • Chen, L., Zhang, L., Greer, P., Tung, P. S. & Moran, M. F. (1993) A murine CDC25/ras-GRF-related protein implicated in Ras regulation. Dev. Genet. 14, 339-346.
    • (1993) Dev. Genet. , vol.14 , pp. 339-346
    • Chen, L.1    Zhang, L.2    Greer, P.3    Tung, P.S.4    Moran, M.F.5
  • 10
    • 0026523616 scopus 로고
    • Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator
    • Martegani, E., Vanoni, M., Zippel, R., Coccetti, P., Brambilla, R., Ferrari, C., Sturani, E. & Alberghina, L. (1992) Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator, Embo J. 11, 2151-2157.
    • (1992) Embo J. , vol.11 , pp. 2151-2157
    • Martegani, E.1    Vanoni, M.2    Zippel, R.3    Coccetti, P.4    Brambilla, R.5    Ferrari, C.6    Sturani, E.7    Alberghina, L.8
  • 11
    • 0028304947 scopus 로고
    • Expression of two different products of CDC25Mm, a mammalian Ras activator, during development of mouse brain
    • Ferrari, C., Zippel, R., Martegani, E., Gnesutta, N., Carrera, V. & Sturani, E. (1994) Expression of two different products of CDC25Mm, a mammalian Ras activator, during development of mouse brain. Exp. Cell Res. 210, 353-357.
    • (1994) Exp. Cell Res. , vol.210 , pp. 353-357
    • Ferrari, C.1    Zippel, R.2    Martegani, E.3    Gnesutta, N.4    Carrera, V.5    Sturani, E.6
  • 12
    • 0029131894 scopus 로고
    • The cellular content of Cdc25p, the Ras exchange factor in Saccharomyces cerevisiae. is regulated by destabilization through a cyclin destruction box
    • Kaplon, T. & Jacquet, M. (1995) The cellular content of Cdc25p, the Ras exchange factor in Saccharomyces cerevisiae. is regulated by destabilization through a cyclin destruction box, J. Biol. Chem. 270, 20 742-20 747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20742-20747
    • Kaplon, T.1    Jacquet, M.2
  • 13
    • 0027054644 scopus 로고
    • Phosphorylation of the S, cerevisiae Cdc25 in response to glucose results in its dissociation from Ras
    • Gross, E., Goldberg, D. & Levitzki, A. (1992) Phosphorylation of the S, cerevisiae Cdc25 in response to glucose results in its dissociation from Ras, Nature 360, 762-765.
    • (1992) Nature , vol.360 , pp. 762-765
    • Gross, E.1    Goldberg, D.2    Levitzki, A.3
  • 14
    • 0029906075 scopus 로고    scopus 로고
    • Membrane-anchoring domains of Cdc25p, a Saccharomyces cerevisiae ras exchange factor
    • Garreau, H., Geymonat, M., Renault, G. & Jacquet, M. (1996) Membrane-anchoring domains of Cdc25p, a Saccharomyces cerevisiae ras exchange factor, Biol. Cell 86, 93-102.
    • (1996) Biol. Cell , vol.86 , pp. 93-102
    • Garreau, H.1    Geymonat, M.2    Renault, G.3    Jacquet, M.4
  • 15
    • 0029115932 scopus 로고
    • Identification of guanine exchange factor key residues involved in exchange activity and Ras interaction
    • Camus, C., Hermann-Le Denmat, S. & Jacquet, M. (1995) Identification of guanine exchange factor key residues involved in exchange activity and Ras interaction, Oncogene 11, 951-959.
    • (1995) Oncogene , vol.11 , pp. 951-959
    • Camus, C.1    Hermann-Le Denmat, S.2    Jacquet, M.3
  • 16
    • 0025158086 scopus 로고
    • The Saccharomyces cerevisiae CDC25 gene product is a 180 kD polypeptide and is associated to a membrane fraction
    • Garreau, H., Camonis, J. H., Guitton, C. & Jacquet, M. (1990) The Saccharomyces cerevisiae CDC25 gene product is a 180 kD polypeptide and is associated to a membrane fraction, FEBS Lett. 269, 53-59.
    • (1990) FEBS Lett. , vol.269 , pp. 53-59
    • Garreau, H.1    Camonis, J.H.2    Guitton, C.3    Jacquet, M.4
  • 17
    • 0026741882 scopus 로고
    • Anti-Cdc2S antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein
    • Gross, E., Marbach, I., Engelberg, D., Segal, M., Simchen, G. & Levitzki, A. (1992) Anti-Cdc2S antibodies inhibit guanyl nucleotide-dependent adenylyl cyclase of Saccharomyces cerevisiae and cross-react with a 150-kilodalton mammalian protein, Mol. Cell. Biol. 12, 2653-2661.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2653-2661
    • Gross, E.1    Marbach, I.2    Engelberg, D.3    Segal, M.4    Simchen, G.5    Levitzki, A.6
  • 18
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interaction
    • Fields, S. & Song, O. (1989) A novel genetic system to detect protein-protein interaction, Nature 340, 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 19
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu. EF-Ts complex at 2.5 Å resolution
    • Kawashima, T., Berthet, C. C., Wulff, M., Cusack, S. & Leberman, R. (1996) The structure of the Escherichia coli EF-Tu. EF-Ts complex at 2.5 Å resolution. Nature 379, 511-518
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet, C.C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 20
    • 0030581475 scopus 로고    scopus 로고
    • Raf gets it together
    • Marshall, C. J. (1996) Raf gets it together, Nature 383, 127-128.
    • (1996) Nature , vol.383 , pp. 127-128
    • Marshall, C.J.1
  • 21
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • Farrar, M. A., Alberola-Ila, J. & Perlmutter, R. M. (1996) Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization, Nature 383, 178-181.
    • (1996) Nature , vol.383 , pp. 178-181
    • Farrar, M.A.1    Alberola-Ila, J.2    Perlmutter, R.M.3
  • 22
    • 0029811985 scopus 로고    scopus 로고
    • Oligomerization activates c-Raf-1 through a Ras-dependent mechanism
    • Luo, Z., Tzivion, G., Belshaw, P. J., Vavvas, D., Marshall, M. & Avruch, J. (1996) Oligomerization activates c-Raf-1 through a Ras-dependent mechanism, Nature 383, 181-185.
    • (1996) Nature , vol.383 , pp. 181-185
    • Luo, Z.1    Tzivion, G.2    Belshaw, P.J.3    Vavvas, D.4    Marshall, M.5    Avruch, J.6
  • 23
    • 0030014844 scopus 로고    scopus 로고
    • Two separate functions are encoded by the carboxyl-terminal domains of the yeast cyclase-associated protein and its mammalian homologs. Dimerization and actin binding
    • Zelicof, A., Protopopov, V., David, D., Lin, X. Y., Lustgarten, V. & Gerst, J. E. (1996) Two separate functions are encoded by the carboxyl-terminal domains of the yeast cyclase-associated protein and its mammalian homologs. Dimerization and actin binding, J. Biol. Chem. 271, 18243-18252.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18243-18252
    • Zelicof, A.1    Protopopov, V.2    David, D.3    Lin, X.Y.4    Lustgarten, V.5    Gerst, J.E.6
  • 24
    • 0027255909 scopus 로고
    • Elimination of false positives that arise in using the two-hybrid system
    • Bartel, P., Chien, C., Sternglanz, R. & Fields, S. (1993) Elimination of false positives that arise in using the two-hybrid system, Bio-Techniques 14, 920-924.
    • (1993) Bio-Techniques , vol.14 , pp. 920-924
    • Bartel, P.1    Chien, C.2    Sternglanz, R.3    Fields, S.4
  • 25
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: Mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer, W., Kleinschmidt, J., Saidowsky, J., Escher, C. & Wolf, D. (1991) Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10, 555-562.
    • (1991) EMBO J. , vol.10 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.2    Saidowsky, J.3    Escher, C.4    Wolf, D.5
  • 26
    • 0000884978 scopus 로고
    • Using the two-hybrid system to detect protein-protein interactions
    • (Hartley, D. A., ed.) Oxford University Press, Oxford
    • Bartel, P., Chien, C., Sternglanz, R. & Fields, S. (1993) Using the two-hybrid system to detect protein-protein interactions, in Cellular interactions in development: a practical approach (Hartley, D. A., ed.) pp. 153-179, Oxford University Press, Oxford.
    • (1993) Cellular Interactions in Development: A Practical Approach , pp. 153-179
    • Bartel, P.1    Chien, C.2    Sternglanz, R.3    Fields, S.4
  • 27
    • 0027953554 scopus 로고
    • Multipurpose vectors designed for the fast generation of N- Or C-terminal epitope-tagged proteins
    • Cullin, C. & Minvielle-Sebastia, L. (1994) Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins. Yeast 10, 105-112.
    • (1994) Yeast , vol.10 , pp. 105-112
    • Cullin, C.1    Minvielle-Sebastia, L.2
  • 28
    • 0028817697 scopus 로고
    • Properties of the catalytic domain of Sdc25p, a yeast GDP/GTP exchange factor of Ras proteins
    • Poullet, P., Créchet, J., Bernardi, A. & Parmeggiani, A. (1995) Properties of the catalytic domain of Sdc25p, a yeast GDP/GTP exchange factor of Ras proteins, Eur. J. Biochem. 227, 537-544.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 537-544
    • Poullet, P.1    Créchet, J.2    Bernardi, A.3    Parmeggiani, A.4
  • 29
    • 0028113581 scopus 로고
    • The ras guanine exchange factor domains of CDC25 and SDC25 differ from that of BUD5, thus allowing to derive subfamilies among CDC25-related GEFs
    • Camus, C., Boy-Marcotte, E. & Jacquet, M (1994) The ras guanine exchange factor domains of CDC25 and SDC25 differ from that of BUD5, thus allowing to derive subfamilies among CDC25-related GEFs, Mol. Gen. Genet. 245, 167-176.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 167-176
    • Camus, C.1    Boy-Marcotte, E.2    Jacquet, M.3
  • 30
    • 0030901637 scopus 로고    scopus 로고
    • Structure of the adenylyl cyclase catalytic core
    • Zhang, G., Liu, Y., Ruoho, A. E. & Hurley, J. H. (1997) Structure of the adenylyl cyclase catalytic core. Nature 386, 247-253.
    • (1997) Nature , vol.386 , pp. 247-253
    • Zhang, G.1    Liu, Y.2    Ruoho, A.E.3    Hurley, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.