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Volumn 119, Issue 5, 1996, Pages 1004-1013

Studies on the phosphorylation of a Mr 25,000 protein, a putative protein phosphatase 2A modulator, by casein kinase I, and analysis of multiple endogenous phosphates

Author keywords

Casein kinase I; Endogenous phosphate; Multisite phosphorylation; Protein phosphorylation; Xenopus laevis oocyte

Indexed keywords

XENOPUS LAEVIS; ANIMALIA;

EID: 0029895490     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021315     Document Type: Article
Times cited : (11)

References (46)
  • 1
    • 0021873606 scopus 로고
    • Regulation of amphibian oocyte maturation
    • Maller, J.L. (1985) Regulation of amphibian oocyte maturation. Cell Differ. 16, 211-221
    • (1985) Cell Differ. , vol.16 , pp. 211-221
    • Maller, J.L.1
  • 2
    • 0024840220 scopus 로고
    • The induction of oocyte maturation: Transmembrane signaling events and regulation of the cell cycle
    • Dennis Smith, L. (1989) The induction of oocyte maturation: Transmembrane signaling events and regulation of the cell cycle. Development 107, 685-699
    • (1989) Development , vol.107 , pp. 685-699
    • Dennis Smith, L.1
  • 3
    • 0017340457 scopus 로고
    • Progesterone-stimulated meiotic cell division in Xenopus oocytes
    • Maller, J.L. and Krebs, E.G. (1977) Progesterone-stimulated meiotic cell division in Xenopus oocytes. J. Biol. Chem. 252, 1712-1718
    • (1977) J. Biol. Chem. , vol.252 , pp. 1712-1718
    • Maller, J.L.1    Krebs, E.G.2
  • 4
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr 160 and Tyr 15
    • Gu, Y., Rosenblatt, J., and Morgan, D.O. (1992) Cell cycle regulation of CDK2 activity by phosphorylation of Thr 160 and Tyr 15. EMBO J. 11, 3995-4005
    • (1992) EMBO J. , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 5
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse, P. (1990) Universal control mechanism regulating onset of M-phase. Nature 344, 503-508
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 6
    • 0028228544 scopus 로고
    • Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation
    • Matten, W., Daar, I., and Vande Woude, G.F. (1994) Protein kinase A acts at multiple points to inhibit Xenopus oocyte maturation. Mol. Cell Biol. 14, 4419-4426
    • (1994) Mol. Cell Biol. , vol.14 , pp. 4419-4426
    • Matten, W.1    Daar, I.2    Vande Woude, G.F.3
  • 7
    • 0028983241 scopus 로고
    • r 25,000 protein, an effective phosphate acceptor for casein kinase II and protein kinase C, detected in the cytosolic fraction of Xenopus laevis oocytes
    • r 25,000 protein, an effective phosphate acceptor for casein kinase II and protein kinase C, detected in the cytosolic fraction of Xenopus laevis oocytes. J. Biochem. 118, 453-460
    • (1995) J. Biochem. , vol.118 , pp. 453-460
    • Hashimoto, E.1    Takeuchi, F.2    Tanaka, Y.3    Yamamura, H.4
  • 8
    • 0023142791 scopus 로고
    • Induction of meiotic maturation in Xenopus oocytes by 12-O-tetradecanoylphorbol 13-acetate
    • Stith, B.J. and Maller, J.L. (1987) Induction of meiotic maturation in Xenopus oocytes by 12-O-tetradecanoylphorbol 13-acetate. Exp. Cell Res. 169, 514-523
    • (1987) Exp. Cell Res. , vol.169 , pp. 514-523
    • Stith, B.J.1    Maller, J.L.2
  • 11
    • 0026039891 scopus 로고
    • Casein kinase I and II-multipotential serine protein kinases: Structure, function and regulation
    • (Greengard, P. and Robison, G.A., eds.) Raven Press, New York
    • Tuazon, P.T. and Traugh, J.A. (1991) Casein kinase I and II-multipotential serine protein kinases: Structure, function and regulation in Advances in Second Messenger and Phosphoprotein Research (Greengard, P. and Robison, G.A., eds.) Vol. 23, pp. 123-164, Raven Press, New York
    • (1991) Advances in Second Messenger and Phosphoprotein Research , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 12
    • 0026093758 scopus 로고
    • Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes
    • Rowles, J., Slaughter, C., Moomaw, C., Hsu, J., and Cobb, M.H. (1991) Purification of casein kinase I and isolation of cDNAs encoding multiple casein kinase I-like enzymes. Proc. Natl. Acad. Sci. USA 88, 9548-9552
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9548-9552
    • Rowles, J.1    Slaughter, C.2    Moomaw, C.3    Hsu, J.4    Cobb, M.H.5
  • 13
    • 0027418069 scopus 로고
    • Molecular cloning, expression, and characterization of a 49-kilodalton casein kinase I isoform from rat testis
    • Graves, P.R., Haas, D.W., Hagedorn, C.H., DePaoli-Roach, A.A., and Roach, P.J. (1993) Molecular cloning, expression, and characterization of a 49-kilodalton casein kinase I isoform from rat testis. J. Biol. Chem. 268, 6394-6401
    • (1993) J. Biol. Chem. , vol.268 , pp. 6394-6401
    • Graves, P.R.1    Haas, D.W.2    Hagedorn, C.H.3    DePaoli-Roach, A.A.4    Roach, P.J.5
  • 17
    • 0028364265 scopus 로고
    • Cytoplasmic forms of fission yeast casein kinase-1 associate primarily with the particulate fraction of the cell
    • Wang, P.-C., Vancura, A., Desai, A., Carmel, G., and Kuret, J. (1994) Cytoplasmic forms of fission yeast casein kinase-1 associate primarily with the particulate fraction of the cell. J. Biol. Chem. 269, 12014-12023
    • (1994) J. Biol. Chem. , vol.269 , pp. 12014-12023
    • Wang, P.-C.1    Vancura, A.2    Desai, A.3    Carmel, G.4    Kuret, J.5
  • 18
    • 0027998364 scopus 로고
    • Molecular cloning and sequence analysis of two novel fission yeast casein kinase-1 isoforms
    • Kearney, P.H., Ebert, M., and Kuret, J. (1994) Molecular cloning and sequence analysis of two novel fission yeast casein kinase-1 isoforms. Biochem. Biophys. Res. Commun. 203, 231-236
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 231-236
    • Kearney, P.H.1    Ebert, M.2    Kuret, J.3
  • 21
    • 0026025503 scopus 로고
    • Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II
    • Cala, S.E. and Jones, L.R. (1991) Phosphorylation of cardiac and skeletal muscle calsequestrin isoforms by casein kinase II. J. Biol. Chem. 266, 391-398
    • (1991) J. Biol. Chem. , vol.266 , pp. 391-398
    • Cala, S.E.1    Jones, L.R.2
  • 22
    • 0013946834 scopus 로고
    • A new micromethod for the colorimetric determination of inorganic phosphate
    • Itaya, K. and Ui, M. (1966) A new micromethod for the colorimetric determination of inorganic phosphate. Clin. Chim. Acta 14, 361-366
    • (1966) Clin. Chim. Acta , vol.14 , pp. 361-366
    • Itaya, K.1    Ui, M.2
  • 23
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • (Neufeld, E.F. and Ginsburg, V., eds.) Academic Press, New York and London
    • Ames, B.N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases in Methods in Enzymology (Neufeld, E.F. and Ginsburg, V., eds.) Vol. 8, pp. 115-118, Academic Press, New York and London
    • (1966) Methods in Enzymology , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophase T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophase T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0024515028 scopus 로고
    • A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide, and affinity purification of casein kinase I from bovine testis
    • Chijiwa, T., Hagiwara, M., and Hidaka, H. (1989) A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide, and affinity purification of casein kinase I from bovine testis. J. Biol. Chem. 264, 4924-4927
    • (1989) J. Biol. Chem. , vol.264 , pp. 4924-4927
    • Chijiwa, T.1    Hagiwara, M.2    Hidaka, H.3
  • 27
    • 0019198966 scopus 로고
    • Inhibition of casein kinase II by heparin
    • Hathaway, G.M., Lubben, T.H., and Traugh, J.A. (1980) Inhibition of casein kinase II by heparin. J. Biol. Chem. 255, 8038-8041
    • (1980) J. Biol. Chem. , vol.255 , pp. 8038-8041
    • Hathaway, G.M.1    Lubben, T.H.2    Traugh, J.A.3
  • 28
    • 0023858859 scopus 로고
    • Inhibition of glycogen synthase (casein) kinase-1 by heparin
    • Singh, T.J. (1988) Inhibition of glycogen synthase (casein) kinase-1 by heparin. Arch. Biochem. Biophys. 260, 661-666
    • (1988) Arch. Biochem. Biophys. , vol.260 , pp. 661-666
    • Singh, T.J.1
  • 30
    • 0026558816 scopus 로고
    • Determinants on simian virus 40 large T antigen are important for recognition and phosphorylation by casein kinase I
    • Umphress, J.L., Tuazon, P.T., Chen, C.-J., and Traugh, J.A. (1992) Determinants on simian virus 40 large T antigen are important for recognition and phosphorylation by casein kinase I. Eur. J. Biochem. 203, 239-243
    • (1992) Eur. J. Biochem. , vol.203 , pp. 239-243
    • Umphress, J.L.1    Tuazon, P.T.2    Chen, C.-J.3    Traugh, J.A.4
  • 31
    • 0025074778 scopus 로고
    • Phosphate groups as substrate determinants for casein kinase I action
    • Flotow, H., Graves, P.R., Wang, A., Fiol, C.J., Roeske, R.W., and Roach, P.J. (1990) Phosphate groups as substrate determinants for casein kinase I action. J. Biol. Chem. 265, 14264-14269
    • (1990) J. Biol. Chem. , vol.265 , pp. 14264-14269
    • Flotow, H.1    Graves, P.R.2    Wang, A.3    Fiol, C.J.4    Roeske, R.W.5    Roach, P.J.6
  • 32
    • 0027258139 scopus 로고
    • Multiple and cooperative phosphorylation events regulate the CREM activator function
    • Groot, R.P., Hertog, J.D., Vandenheede, J.R., Goris, J., and Sassone-Corsi, P. (1993) Multiple and cooperative phosphorylation events regulate the CREM activator function. EMBO J. 12, 3903-3911
    • (1993) EMBO J. , vol.12 , pp. 3903-3911
    • Groot, R.P.1    Hertog, J.D.2    Vandenheede, J.R.3    Goris, J.4    Sassone-Corsi, P.5
  • 33
    • 0019888345 scopus 로고
    • The structure of vitellogenin
    • Wiley, H.S. and Wallace, R.A. (1981) The structure of vitellogenin. J. Biol. Chem. 256, 8626-8634
    • (1981) J. Biol. Chem. , vol.256 , pp. 8626-8634
    • Wiley, H.S.1    Wallace, R.A.2
  • 35
    • 0019474508 scopus 로고
    • Vitellogenesis and the vitellogenin gene family
    • Wahli, W., Dawid, I.B., Ryffel, G.U., and Weber, R. (1981) Vitellogenesis and the vitellogenin gene family. Science 212, 298-304
    • (1981) Science , vol.212 , pp. 298-304
    • Wahli, W.1    Dawid, I.B.2    Ryffel, G.U.3    Weber, R.4
  • 36
    • 0023664563 scopus 로고
    • Precursor-product relationship between vitellogenin and the yolk proteins as derived from the complete sequence of a Xenopus vitellogenin gene
    • Gerber-Huber, S., Nardelli, D., Haefliger, J.-A., Cooper, D.N., Givel, F., Germond, J.-E., Engel, J., Green, N.M., and Wahli, W. (1987) Precursor-product relationship between vitellogenin and the yolk proteins as derived from the complete sequence of a Xenopus vitellogenin gene. Nucleic Acids Res. 15, 4737-4760
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4737-4760
    • Gerber-Huber, S.1    Nardelli, D.2    Haefliger, J.-A.3    Cooper, D.N.4    Givel, F.5    Germond, J.-E.6    Engel, J.7    Green, N.M.8    Wahli, W.9
  • 37
    • 0026321413 scopus 로고
    • Multisite and hierarchal protein phosphorylation
    • Roach, P.J. (1991) Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266, 14139-14142
    • (1991) J. Biol. Chem. , vol.266 , pp. 14139-14142
    • Roach, P.J.1
  • 38
    • 0025202408 scopus 로고
    • Control of glycogen synthase by hierarchal protein phosphorylation
    • Roach, P.J. (1990) Control of glycogen synthase by hierarchal protein phosphorylation. FASEB J. 4, 2961-2968
    • (1990) FASEB J. , vol.4 , pp. 2961-2968
    • Roach, P.J.1
  • 39
    • 0026040191 scopus 로고
    • Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases
    • Kennelly, P.J. and Krebs, E.G. (1991) Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J. Biol. Chem. 266, 15555-15558
    • (1991) J. Biol. Chem. , vol.266 , pp. 15555-15558
    • Kennelly, P.J.1    Krebs, E.G.2
  • 40
    • 0024510685 scopus 로고
    • Mechanism of phosphorylation in the lumen of the Golgi apparatus
    • Capasso, J.M., Keenan, T.W., Abeijon, C., and Hirschberg, C.B. (1989) Mechanism of phosphorylation in the lumen of the Golgi apparatus. J. Biol. Chem. 264, 5233-5240
    • (1989) J. Biol. Chem. , vol.264 , pp. 5233-5240
    • Capasso, J.M.1    Keenan, T.W.2    Abeijon, C.3    Hirschberg, C.B.4
  • 41
    • 0028913538 scopus 로고
    • Crystal structure of casein kinase-1, a phosphate-directed protein kinase
    • Xu, R.-M., Carmel, G., Sweet, R.M., Kuret, J., and Cheng, X.-D. (1995) Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 14, 1015-1023
    • (1995) EMBO J. , vol.14 , pp. 1015-1023
    • Xu, R.-M.1    Carmel, G.2    Sweet, R.M.3    Kuret, J.4    Cheng, X.-D.5
  • 42
    • 0021162965 scopus 로고
    • A/GSK-3 and casein kinase II (PC 0.7)
    • A/GSK-3 and casein kinase II (PC 0.7). J. Biol. Chem. 259, 12144-12152
    • (1984) J. Biol. Chem. , vol.259 , pp. 12144-12152
    • DePaoli-Roach, A.A.1
  • 44
    • 0028916490 scopus 로고
    • Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo
    • Desdouits, F., Cohen, D., Nairn, A.C., Greengard, P., and Girault, J.-A. (1995) Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo. J. Biol. Chem. 270, 8772-8778
    • (1995) J. Biol. Chem. , vol.270 , pp. 8772-8778
    • Desdouits, F.1    Cohen, D.2    Nairn, A.C.3    Greengard, P.4    Girault, J.-A.5
  • 45
    • 0027296041 scopus 로고
    • The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues
    • Fesquet, D., Labbé, J.-C., Derancourt, J., Capony, J.-P., Galas, S., Girard, F., Lorca, T., Shuttleworth, J., Dorée, M., and Cavadore, J.-C. (1993) The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J. 12, 3111-3121
    • (1993) EMBO J. , vol.12 , pp. 3111-3121
    • Fesquet, D.1    Labbé, J.-C.2    Derancourt, J.3    Capony, J.-P.4    Galas, S.5    Girard, F.6    Lorca, T.7    Shuttleworth, J.8    Dorée, M.9    Cavadore, J.-C.10
  • 46
    • 0029877915 scopus 로고    scopus 로고
    • r 25,000 protein, a putative protein phosphatase 2A modulator, and phosphorylation of the synthetic peptide containing these sites by protein kinase C
    • r 25,000 protein, a putative protein phosphatase 2A modulator, and phosphorylation of the synthetic peptide containing these sites by protein kinase C. J. Biochem. 119, 626-632
    • (1996) J. Biochem. , vol.119 , pp. 626-632
    • Hashimoto, E.1    Kobayashi, N.2    Kubota, N.3    Tanaka, Y.4    Yamamura, H.5


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