메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 519-528

The recombinant a isoform of protein kinase CK1 from Xenopus laevis can phosphorylate tyrosine in synthetic substrates

Author keywords

Casein kinase 1; Poly(glutamic acid, tyrosine); Tyrosine phosphorylation

Indexed keywords

BOVINAE; ESCHERICHIA COLI; XENOPUS LAEVIS; ANIMALIA; BOS TAURUS;

EID: 0030438629     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0519r.x     Document Type: Article
Times cited : (21)

References (43)
  • 1
    • 0028007154 scopus 로고
    • Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine and tyrosine
    • Ali, N., Hakfter, U. & Chua, N. H. (1994) Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine and tyrosine, J. Biol. Chem. 269, 31 626-31 629.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31626-31629
    • Ali, N.1    Hakfter, U.2    Chua, N.H.3
  • 2
    • 0028871365 scopus 로고
    • Casein kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis
    • Beyaert, R., Vanhaesebroeck, B., Declercq, W., Van Lint, J., Vandenabeele, P., Agostinis, P., Vandenheede, J. R. & Fiers, W. (1995) Casein kinase-1 phosphorylates the p75 tumor necrosis factor receptor and negatively regulates tumor necrosis factor signaling for apoptosis, J. Biol. Chem. 270, 23 293-23 299.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23293-23299
    • Beyaert, R.1    Vanhaesebroeck, B.2    Declercq, W.3    Van Lint, J.4    Vandenabeele, P.5    Agostinis, P.6    Vandenheede, J.R.7    Fiers, W.8
  • 3
    • 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
  • 4
    • 0021341961 scopus 로고
    • Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases
    • Braun, S., Raymond, W. E. & Racker, E. (1984) Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases, J. Biol. Chem. 259, 2051-1054.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2051-11054
    • Braun, S.1    Raymond, W.E.2    Racker, E.3
  • 6
    • 0019876755 scopus 로고
    • Purification and properties of calf thymus casein kinases I and II
    • Dahmus, M. E. (1981) Purification and properties of calf thymus casein kinases I and II, J. Biol. Chem. 256, 3319-3325.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3319-3325
    • Dahmus, M.E.1
  • 9
    • 0029036113 scopus 로고
    • Isolation and characterization of human casein kinase Iε (CKI), a novel member of the CKI gene family
    • Fish, K. J., Gegielska, A., Getman, M. E., Landes, G. M. & Virshup, D. M. (1995) Isolation and characterization of human casein kinase Iε (CKI), a novel member of the CKI gene family, J. Biol. Chem. 270, 14 875-14 883.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14875-14883
    • Fish, K.J.1    Gegielska, A.2    Getman, M.E.3    Landes, G.M.4    Virshup, D.M.5
  • 10
    • 0025731508 scopus 로고
    • Role of acidic residues as substrate determinants for casein kinase I
    • Flotow, H. & Roach, P. J. (1991) Role of acidic residues as substrate determinants for casein kinase I, J. Biol. Chem. 266, 3724-3727.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3724-3727
    • Flotow, H.1    Roach, P.J.2
  • 12
    • 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., De Paoli-Roach, A. A. & 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    De Paoli-Roach, A.A.4    Roach, P.J.5
  • 13
    • 0029131396 scopus 로고
    • Role of COOH-terminal phosphorylation in the regulation of casein kinase Iδ
    • Graves, P. R. & Roach, P. J. (1995) Role of COOH-terminal phosphorylation in the regulation of casein kinase Iδ, J. Biol. Chem. 270, 21 689-21 694.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21689-21694
    • Graves, P.R.1    Roach, P.J.2
  • 14
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K. & Quinn, A. M. (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members, Methods Enzymol. 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 15
    • 0020437026 scopus 로고
    • Casein kinases-multipotential protein kinases
    • (Stadman, E. & Horecker, B., eds) Academic Press, New York
    • Hathaway, G. M. & Traugh, J. A. (1982) Casein kinases-multipotential protein kinases, in Current topics in cellular regulation (Stadman, E. & Horecker, B., eds) vol. 21, pp. 101-127, Academic Press, New York.
    • (1982) Current Topics in Cellular Regulation , vol.21 , pp. 101-127
    • Hathaway, G.M.1    Traugh, J.A.2
  • 18
    • 0027430998 scopus 로고
    • Casein kinases; pleiotropic mediators of cellular regulation
    • Issinger, O.-G. (1993) Casein kinases; pleiotropic mediators of cellular regulation, Pharmacol. Ther. 591, 1-30.
    • (1993) Pharmacol. Ther. , vol.591 , pp. 1-30
    • Issinger, O.-G.1
  • 19
    • 0029379570 scopus 로고
    • Multiple isoforms of Arabidopsis casein kinase 1 combine conserved catalytic domains with variable carboxyl-terminal extensions
    • Klimczak, L. J., Farini, D., Lin, C., Ponti, D., Cashmore, A. R. & Giuliano, G. (1995) Multiple isoforms of Arabidopsis casein kinase 1 combine conserved catalytic domains with variable carboxyl-terminal extensions, Plant Physiol. 109, 687-696.
    • (1995) Plant Physiol. , vol.109 , pp. 687-696
    • Klimczak, L.J.1    Farini, D.2    Lin, C.3    Ponti, D.4    Cashmore, A.R.5    Giuliano, G.6
  • 20
    • 46149136123 scopus 로고
    • Genetics of Polyploid Xenopus
    • Kobel, H. R. & Du Pasquier, L. (1986) Genetics of Polyploid Xenopus, Trends Genet. 2, 310-315.
    • (1986) Trends Genet. , vol.2 , pp. 310-315
    • Kobel, H.R.1    Du Pasquier, L.2
  • 21
    • 0029963896 scopus 로고    scopus 로고
    • Three dimensional structure of mammalian casein kinase I: Molecular basis for phosphate recognition
    • Longenechker, K. L., Roach, P. & Hurley, T. D. (1996) Three dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition, J. Mol. Biol. 257, 618-631.
    • (1996) J. Mol. Biol. , vol.257 , pp. 618-631
    • Longenechker, K.L.1    Roach, P.2    Hurley, T.D.3
  • 22
    • 0028016444 scopus 로고
    • Phosphorylation of synthetic fragments of inhibitor-2 of protein phosphatase-1 by casein kinase-1 and-2
    • Marin, O., Meggio, F., Sarno, S., Andretta, M. & Pinna, L. A. (1994) Phosphorylation of synthetic fragments of inhibitor-2 of protein phosphatase-1 by casein kinase-1 and-2, Eur. J. Biochem. 223, 647-653.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 647-653
    • Marin, O.1    Meggio, F.2    Sarno, S.3    Andretta, M.4    Pinna, L.A.5
  • 23
    • 0024529477 scopus 로고
    • Random tyrosine and glutamic acid-containing polymers are very powerful inhibitors of casein kinase-2
    • Meggio, F. & Pinna, L. A. (1989) Random tyrosine and glutamic acid-containing polymers are very powerful inhibitors of casein kinase-2, Biochem. Biophys. Acta 1010, 128-130.
    • (1989) Biochem. Biophys. Acta , vol.1010 , pp. 128-130
    • Meggio, F.1    Pinna, L.A.2
  • 24
    • 0025801732 scopus 로고
    • A synthetic β-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase
    • Meggio, P., Perich, J. W., Reynolds, E. C. & Pinna, L. A. (1991) A synthetic β-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase, FEBS Lett. 283, 303-306.
    • (1991) FEBS Lett. , vol.283 , pp. 303-306
    • Meggio, P.1    Perich, J.W.2    Reynolds, E.C.3    Pinna, L.A.4
  • 25
    • 0026663552 scopus 로고
    • Phosphorylation of the p53 tumor suppressor protein at three N-terminal sites by novel casein kinase I-like enzyme
    • Milne, D. M., Palmer, R. H., Campbell, D. G. & Meek, D. W. (1992) Phosphorylation of the p53 tumor suppressor protein at three N-terminal sites by novel casein kinase I-like enzyme, Oncogene 7, 1361-1369.
    • (1992) Oncogene , vol.7 , pp. 1361-1369
    • Milne, D.M.1    Palmer, R.H.2    Campbell, D.G.3    Meek, D.W.4
  • 26
    • 0025133304 scopus 로고
    • An alternative method for a fast separation of phosphotyrosine
    • Muñoz, G. & Marshall, S. H. (1990) An alternative method for a fast separation of phosphotyrosine, Anal. Biochem. 190, 233-237.
    • (1990) Anal. Biochem. , vol.190 , pp. 233-237
    • Muñoz, G.1    Marshall, S.H.2
  • 27
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson, T. & Schlessinger, J. (1995) Protein modules and signalling networks, Nature 373, 573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1    Schlessinger, J.2
  • 28
    • 0022133045 scopus 로고
    • Identification and cloning of localized maternal RNAs from Xenopus eggs
    • abagliati, M., Weeks, D., Harvey, R. & Melton, D, (1985) Identification and cloning of localized maternal RNAs from Xenopus eggs, Cell 42, 769-777.
    • (1985) Cell , vol.42 , pp. 769-777
    • Abagliati, M.1    Weeks, D.2    Harvey, R.3    Melton, D.4
  • 29
    • 0025815287 scopus 로고
    • Phosphorylation of the insulin receptor by a casein kinase I-like enzyme
    • Rapuano, M. & Rosen, O. M. (1991) Phosphorylation of the insulin receptor by a casein kinase I-like enzyme, J. Biol. Chem. 266, 12 902-12 907.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12902-12907
    • Rapuano, M.1    Rosen, O.M.2
  • 30
    • 0026093758 scopus 로고
    • Purification of casein kinase I and isolation of cDNAs encoding multiple casein I-like enzymes
    • Rowles, J., Slaughter, C., Moomaw, C., Hsu, J. & Cobb, M. (1991) Purification of casein kinase I and isolation of cDNAs encoding multiple casein 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.5
  • 33
    • 0029931327 scopus 로고    scopus 로고
    • The casein kinase 1α gene of Drosophila melanogaster is developmentally regulated and the kinase activity of the protein induced by DNA damage
    • Santos, J. A., Logarinho, E., Tapia, C., Allende, C. C., Allende, J. E. & Sunkel, C. E. (1996) The casein kinase 1α gene of Drosophila melanogaster is developmentally regulated and the kinase activity of the protein induced by DNA damage, J. Cell Sci, 109, 1847-1856.
    • (1996) J. Cell Sci , vol.109 , pp. 1847-1856
    • Santos, J.A.1    Logarinho, E.2    Tapia, C.3    Allende, C.C.4    Allende, J.E.5    Sunkel, C.E.6
  • 34
    • 0022608294 scopus 로고
    • Protein tyrosyne kinase activity in Sacharomyces cerevisiae
    • Schieven, G., Thorner, J. & Martin, G. S. (1986) Protein tyrosyne kinase activity in Sacharomyces cerevisiae, Science 231, 390-393.
    • (1986) Science , vol.231 , pp. 390-393
    • Schieven, G.1    Thorner, J.2    Martin, G.S.3
  • 35
    • 0023806075 scopus 로고
    • Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione s-transferase
    • Smith, D. B. & Johnson, K. S. (1988) Single step purification of polypeptides expressed in Escherichia coli as fusions with glutathione s-transferase, Gene (Amst.) 67, 31-38.
    • (1988) Gene (Amst.) , vol.67 , pp. 31-38
    • Smith, D.B.1    Johnson, K.S.2
  • 38
    • 0025353028 scopus 로고
    • Copolymers of glutamic acid and tyrosine are potent inhibitors of oocyte casein kinase II
    • Téllez, R., Gatica, M., Allende, C. C. & Allende, J. E. (1990) Copolymers of glutamic acid and tyrosine are potent inhibitors of oocyte casein kinase II, FEBS Lett. 265, 113-116.
    • (1990) FEBS Lett. , vol.265 , pp. 113-116
    • Téllez, R.1    Gatica, M.2    Allende, C.C.3    Allende, J.E.4
  • 39
    • 0022985885 scopus 로고
    • Regulation of protein synthesis by phosphorylation of ribosomal protein S6 and aminoacyl-tRNA synthetases
    • Traugh, J. A. & Pendergast, A. M. (1986) Regulation of protein synthesis by phosphorylation of ribosomal protein S6 and aminoacyl-tRNA synthetases, Progr. Nucleic Acids Res. Mol. Biol. 33, 195-230.
    • (1986) Progr. Nucleic Acids Res. Mol. Biol. , vol.33 , pp. 195-230
    • Traugh, J.A.1    Pendergast, A.M.2
  • 40
    • 0026039891 scopus 로고
    • Casein kinase I and II - Multipotential serine protein kinases: Structure, function and regulation
    • Tuazon, P. T. & Traugh, J. A. (1991) Casein kinase I and II - multipotential serine protein kinases: structure, function and regulation, Adv. Second Messenger Phosphoprot. Res. 23, 123-164.
    • (1991) Adv. Second Messenger Phosphoprot. Res. , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 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. & Chen, X. (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    Chen, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.