메뉴 건너뛰기




Volumn 12, Issue 8, 1992, Pages 3460-3469

Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0026637095     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.12.8.3460     Document Type: Article
Times cited : (207)

References (61)
  • 2
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated used of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., L. Cao, and N. Kleckner. 1987. A method for gene disruption that allows repeated used of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116: 541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 4
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • Becker, D. M., and L. Guarente. 1991. High-efficiency transformation of yeast by electroporation. Methods Enzymol. 194:182-187.
    • (1991) Methods Enzymol. , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 5
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink. 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 6
    • 0020201569 scopus 로고
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle
    • 2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle. Proc. Natl. Acad. Sci. USA 79:6128-6131.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6128-6131
    • Carr, S.A.1    Biemann, K.2    Shoji, S.3    Parmalee, D.C.4    Tatani, K.5
  • 7
    • 0020808608 scopus 로고
    • Extracellular suppression allows mating by pheromone-deficient sterile mutants of Saccharomyces cerevisiae
    • Chan, R. K., L. M. Melnick, L. C. Blair, and J. Thorner. 1983. Extracellular suppression allows mating by pheromone-deficient sterile mutants of Saccharomyces cerevisiae. J. Bacteriol. 155:903-906.
    • (1983) J. Bacteriol. , vol.155 , pp. 903-906
    • Chan, R.K.1    Melnick, L.M.2    Blair, L.C.3    Thorner, J.4
  • 8
    • 0022965871 scopus 로고
    • Separation of large DNA molecules by contour-clamped homogeneous electric fields
    • Chu, G., D. Vollrath, and R. W. Davis. 1986. Separation of large DNA molecules by contour-clamped homogeneous electric fields. Science 234:1582-1585.
    • (1986) Science , vol.234 , pp. 1582-1585
    • Chu, G.1    Vollrath, D.2    Davis, R.W.3
  • 9
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen, P. 1989. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58:453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 10
    • 0024375682 scopus 로고
    • Remarkable similarities between yeast and mammalian protein phosphatases
    • Cohen, P., D. L. Schelling, and M. J. R. Stark. 1989. Remarkable similarities between yeast and mammalian protein phosphatases. FEBS Lett. 250:601-606.
    • (1989) FEBS Lett. , vol.250 , pp. 601-606
    • Cohen, P.1    Schelling, D.L.2    Stark, M.J.R.3
  • 11
    • 85033630315 scopus 로고    scopus 로고
    • Unpublished data
    • Cyert, M. S. Unpublished data.
    • Cyert, M.S.1
  • 12
    • 0003843015 scopus 로고
    • Immunosuppressants hit the target
    • Cyert, M. S. 1992. Immunosuppressants hit the target. Curr. Biol. 2:18-20.
    • (1992) Curr. Biol. , vol.2 , pp. 18-20
    • Cyert, M.S.1
  • 14
    • 0025913953 scopus 로고
    • Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase
    • Cyert, M. S., R. Kunisawa, D. Kaim, and J. Thorner. 1991. Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase. Proc. Natl. Acad. Sci. USA 88:7376-7380.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7376-7380
    • Cyert, M.S.1    Kunisawa, R.2    Kaim, D.3    Thorner, J.4
  • 15
    • 25344435809 scopus 로고
    • Identification of a calcineurin-like activity in the yeast Saccharomyces cerevisiae
    • Cyert, M. S., and J. Thorner. 1988. Identification of a calcineurin-like activity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 107:841a.
    • (1988) J. Cell Biol. , vol.107
    • Cyert, M.S.1    Thorner, J.2
  • 16
    • 0024313794 scopus 로고
    • Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable
    • Davis, T. N., and J. Thorner. 1989. Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable. Proc. Natl. Acad. Sci. USA 86:7909-7913.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7909-7913
    • Davis, T.N.1    Thorner, J.2
  • 17
    • 0023006881 scopus 로고
    • Isolation of the yeast calmodulin gene: Calmodulin is an essential protein
    • Davis, T. N., M. S. Urdea, F. R. Masiarz, and J. Thorner. 1986. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47:423-431.
    • (1986) Cell , vol.47 , pp. 423-431
    • Davis, T.N.1    Urdea, M.S.2    Masiarz, F.R.3    Thorner, J.4
  • 18
    • 0024590280 scopus 로고
    • Disruption of the yeast N-myristoyl transferase gene causes recessive lethality
    • Duronio, R. J., D. A. Towler, R. O. Heuckeroth, and J. I. Gordon. 1989. Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science 243:796-800.
    • (1989) Science , vol.243 , pp. 796-800
    • Duronio, R.J.1    Towler, D.A.2    Heuckeroth, R.O.3    Gordon, J.I.4
  • 19
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-13.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 20
    • 0025831980 scopus 로고
    • Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: One in the presence and one in the absence of CsA
    • Friedman, J., and I. Weissman. 1991. Two cytoplasmic candidates for immunophilin action are revealed by affinity for a new cyclophilin: one in the presence and one in the absence of CsA. Cell 66:799-806.
    • (1991) Cell , vol.66 , pp. 799-806
    • Friedman, J.1    Weissman, I.2
  • 21
    • 0024358139 scopus 로고
    • Cloning of human calcineurin A: Evidence for two isozymes and identification of a polyproline structural domain
    • Guerini, D., and C. B. Klee. 1989. Cloning of human calcineurin A: evidence for two isozymes and identification of a polyproline structural domain. Proc. Natl. Acad. Sci. USA 86:9183-9187.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9183-9187
    • Guerini, D.1    Klee, C.B.2
  • 24
    • 0025963054 scopus 로고
    • Putting the HO gene to work: Practical uses for mating-type switching
    • Herskowitz, I., and R. E. Jensen. 1991. Putting the HO gene to work: practical uses for mating-type switching. Methods Enzymol. 194:132-146.
    • (1991) Methods Enzymol. , vol.194 , pp. 132-146
    • Herskowitz, I.1    Jensen, R.E.2
  • 25
    • 0026001746 scopus 로고
    • Calmodulin-dependent protein phosphatase from Neurospora crassa. Molecular cloning and expression of recombinant catalytic subunit
    • Higuchi, S., J. Tamura, R. Giri, J. W. Polli, and R. L. Kincaid. 1991. Calmodulin-dependent protein phosphatase from Neurospora crassa. Molecular cloning and expression of recombinant catalytic subunit. J. Biol. Chem. 266:18104-18112.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18104-18112
    • Higuchi, S.1    Tamura, J.2    Giri, R.3    Polli, J.W.4    Kincaid, R.L.5
  • 26
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill, J. E., A. M. Myers, J. J. Koerner, and A. Tzagaloff. 1986. Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast 2:163-167.
    • (1986) Yeast , vol.2 , pp. 163-167
    • Hill, J.E.1    Myers, A.M.2    Koerner, J.J.3    Tzagaloff, A.4
  • 27
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C. S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli. Gene 57:267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 28
    • 0025324408 scopus 로고
    • i rise in maintaining viability of yeast cells late in the mating pheromone response pathway
    • i rise in maintaining viability of yeast cells late in the mating pheromone response pathway. J. Biol. Chem. 265:13391-13399.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13391-13399
    • Iida, H.1    Yagawa, Y.2    Anraku, Y.3
  • 29
    • 0024376509 scopus 로고
    • The complete primary structure of calcineurin A, a calmodulin binding protein homologous with protein phosphatases 1 and 2A
    • Ito, A., T. Hashimoto, M. Hirai, T. Takeda, H. Shuntoh, T. Kuno, and C. Tanaka. 1989. The complete primary structure of calcineurin A, a calmodulin binding protein homologous with protein phosphatases 1 and 2A. Biochem. Biophys. Res. Commun. 163:1492-1497.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 1492-1497
    • Ito, A.1    Hashimoto, T.2    Hirai, M.3    Takeda, T.4    Shuntoh, H.5    Kuno, T.6    Tanaka, C.7
  • 30
    • 0025974219 scopus 로고
    • Tackling the protease problem in Saccharomyces cerevisiae
    • Jones, E. W. 1991. Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol. 194:428-453.
    • (1991) Methods Enzymol. , vol.194 , pp. 428-453
    • Jones, E.W.1
  • 33
    • 85033623700 scopus 로고    scopus 로고
    • The pheromone signal pathway in Saccharomyces cerevisiae
    • in press
    • Konopka, J. B., and S. Fields. The pheromone signal pathway in Saccharomyces cerevisiae. Antonie Leeuwenhoek, in press.
    • Antonie Leeuwenhoek
    • Konopka, J.B.1    Fields, S.2
  • 34
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger, R. H. 1980. Structure and evolution of calcium-modulated proteins. Crit. Rev. Biochem. 8:119-174.
    • (1980) Crit. Rev. Biochem. , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 35
    • 0024820182 scopus 로고
    • Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A)
    • Kuno, T., T. Takeda, M. Hirai, A. Ito, H. Mukai, and C. Tanaka. 1989. Evidence for a second isoform of the catalytic subunit of calmodulin-dependent protein phosphatase (calcineurin A). Biochem. Biophys. Res. Commun. 165:1352-1358.
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 1352-1358
    • Kuno, T.1    Takeda, T.2    Hirai, M.3    Ito, A.4    Mukai, H.5    Tanaka, C.6
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 277:680-684.
    • (1970) Nature (London) , vol.277 , pp. 680-684
    • Laemmli, U.1
  • 39
    • 0025860959 scopus 로고
    • Physical map of the Saccharomyces cerevisiae genome at 110-kilobase resolution
    • Link, A. J., and M. V. Olson. 1991. Physical map of the Saccharomyces cerevisiae genome at 110-kilobase resolution. Genetics 127:681-698.
    • (1991) Genetics , vol.127 , pp. 681-698
    • Link, A.J.1    Olson, M.V.2
  • 40
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-CsA and FKBP-FK506 complexes
    • Liu, J., J. D. Farmer, Jr., W. L. Lane, J. Friedman, I. Weissman, and S. L. Schreiber. 1991. Calcineurin is a common target of cyclophilin-CsA and FKBP-FK506 complexes. Cell 66:807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.L.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 41
    • 0025809351 scopus 로고
    • The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B
    • Liu, Y., S. Ishii, M. Tokai, H. Tsutsumi, O. Ohke, R. Akada, K. Tanaka, E. Tsucbiya, S. Fukui, and T. Miyakawa. 1991. The Saccharomyces cerevisiae genes (CMP1 and CMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B. Mol. Gen. Genet. 227: 52-59.
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 52-59
    • Liu, Y.1    Ishii, S.2    Tokai, M.3    Tsutsumi, H.4    Ohke, O.5    Akada, R.6    Tanaka, K.7    Tsucbiya, E.8    Fukui, S.9    Miyakawa, T.10
  • 42
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after SDS gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after SDS gel electrophoresis. J. Biochem. 95:511-519.
    • (1984) J. Biochem. , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 43
    • 0022183368 scopus 로고
    • Bovine brain calmodulin-dependent protein phosphatase
    • Merat, D. L., Z. Y. Hu, T. E. Carter, and W. Y. Cheung. 1985. Bovine brain calmodulin-dependent protein phosphatase. J. Biol. Chem. 260:11053-11059.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11053-11059
    • Merat, D.L.1    Hu, Z.Y.2    Carter, T.E.3    Cheung, W.Y.4
  • 44
    • 0023376810 scopus 로고
    • Exocytosis induction in Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: Possible involvement of calcineurin in exocytic membrane fusion
    • Momayezi, M., C. J. Lumpert, H. Kersken, U. Gras, H. Plattner, M. H. Krinks, and C. B. Klee. 1987. Exocytosis induction in Paramecium tetraurelia cells by exogenous phosphoprotein phosphatase in vivo and in vitro: possible involvement of calcineurin in exocytic membrane fusion. J. Cell Biol. 105:181-189.
    • (1987) J. Cell Biol. , vol.105 , pp. 181-189
    • Momayezi, M.1    Lumpert, C.J.2    Kersken, H.3    Gras, U.4    Plattner, H.5    Krinks, M.H.6    Klee, C.B.7
  • 47
    • 0021991256 scopus 로고
    • Subunit phosphorylation and activation of skeletal muscle phosphorylase kinase by the cAMP-dependent protein kinase
    • Pickett-Gies, C. A., and D. A. Walsh. 1985. Subunit phosphorylation and activation of skeletal muscle phosphorylase kinase by the cAMP-dependent protein kinase. J. Biol. Chem. 260: 2046-2056.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2046-2056
    • Pickett-Gies, C.A.1    Walsh, D.A.2
  • 48
    • 0024294018 scopus 로고
    • The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain
    • Reneke, J. E., K. J. Blumer, W. E. Courchesne, and J. Thorner. 1988. The carboxy-terminal segment of the yeast alpha-factor receptor is a regulatory domain. Cell 55:221-234.
    • (1988) Cell , vol.55 , pp. 221-234
    • Reneke, J.E.1    Blumer, K.J.2    Courchesne, W.E.3    Thorner, J.4
  • 51
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 52
    • 0024819250 scopus 로고
    • Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli
    • Slice, L. W., and S. S. Taylor. 1989. Expression of the catalytic subunit of cAMP-dependent protein kinase in Escherichia coli. J. Biol. Chem. 264:20940-20946.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20940-20946
    • Slice, L.W.1    Taylor, S.S.2
  • 53
    • 0023461432 scopus 로고
    • Lambda gt11: Gene isolation with antibody probes and other applications
    • Snyder, M., S. Elledge, D. Sweetser, R. A. Young, and R. W. Davis. 1987. Lambda gt11: gene isolation with antibody probes and other applications. Methods Enzymol. 154:107-128.
    • (1987) Methods Enzymol. , vol.154 , pp. 107-128
    • Snyder, M.1    Elledge, S.2    Sweetser, D.3    Young, R.A.4    Davis, R.W.5
  • 54
    • 0025992278 scopus 로고
    • Signal transduction in yeast mating
    • Sprague, G. F., Jr. 1991. Signal transduction in yeast mating. Trends Genet. 7:393-397.
    • (1991) Trends Genet. , vol.7 , pp. 393-397
    • Sprague Jr., G.F.1
  • 55
    • 0025937311 scopus 로고
    • α protein of yeast: Conditional activation of the pheromone response by a temperature-sensitive N-myristoyltransferase
    • α protein of yeast: conditional activation of the pheromone response by a temperature-sensitive N-myristoyltransferase. Genes Dev. 5:1969-1981.
    • (1991) Genes Dev. , vol.5 , pp. 1969-1981
    • Stone, D.E.1    Cole, G.M.2    De Barros Lopes, M.3    Goebl, M.4    Reed, S.I.5
  • 56
    • 0023952125 scopus 로고
    • Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm
    • Tash, J. S., M. Krinks, J. Patel, R. L. Means, C. B. Klee, and A. R. Means. 1988. Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J. Cell Biol. 106:1625-1633.
    • (1988) J. Cell Biol. , vol.106 , pp. 1625-1633
    • Tash, J.S.1    Krinks, M.2    Patel, J.3    Means, R.L.4    Klee, C.B.5    Means, A.R.6
  • 57
    • 0025086823 scopus 로고
    • Regulation of organelle transport in melanophores
    • Thaler, C. D., and L. T. Haimo. 1990. Regulation of organelle transport in melanophores. J. Cell Biol. 111:1939-1948.
    • (1990) J. Cell Biol. , vol.111 , pp. 1939-1948
    • Thaler, C.D.1    Haimo, L.T.2
  • 58
    • 0009482260 scopus 로고
    • A procedure for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets and some applications
    • Towbin, H. T., T. Staehelin, and J. Gordon. 1979. A procedure for the electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehelin, T.2    Gordon, J.3
  • 59
  • 60
    • 0024763496 scopus 로고
    • Nuclear pre-mRNA splicing in yeast
    • Woolford, J. L. 1989. Nuclear pre-mRNA splicing in yeast. Yeast 5:439-457.
    • (1989) Yeast , vol.5 , pp. 439-457
    • Woolford, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.