메뉴 건너뛰기




Volumn 239, Issue 1, 1996, Pages 183-189

Characterization of a ribosomal inhibitory polypeptide of protein phosphatase-1 from rat liver

Author keywords

Dephosphorylation; Protein phosphatase; Ribosome

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE;

EID: 0029896654     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0183u.x     Document Type: Article
Times cited : (24)

References (34)
  • 1
    • 0026695872 scopus 로고
    • The structure, role, and regulation of type-1 protein phosphatases
    • Bollen, M. & Stalmans, W. (1992) The structure, role, and regulation of type-1 protein phosphatases, Crit. Rev. Biochem. Mol. Biol. 27, 227-281.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 227-281
    • Bollen, M.1    Stalmans, W.2
  • 2
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera, S. & Hemmings, B. A. (1995) Serine/threonine protein phosphatases, Biochem. J. 311, 17-29.
    • (1995) Biochem. J. , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 3
    • 0026671202 scopus 로고
    • The isolation of novel inhibitory polypeptides of protein phosphatase-1 from bovine thymus nuclei
    • Beullens, M., Van Eynde, A., Stalmans, W. & Bollen, M. (1992) The isolation of novel inhibitory polypeptides of protein phosphatase-1 from bovine thymus nuclei. J. Biol. Chem. 267, 16538-16544.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16538-16544
    • Beullens, M.1    Van Eynde, A.2    Stalmans, W.3    Bollen, M.4
  • 4
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard, M. J. & Cohen, P. (1993) On target with a new mechanism for the regulation of protein phosphorylation, Trends Biochem. Sci. 18, 172-177.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 5
    • 0023691932 scopus 로고
    • Distinct type-1 protein phosphatases are associated with hepatic glycogen and microsomes
    • Schelling, D., Leader, D. P., Zammit, V. A. & Cohen, P. (1988) Distinct type-1 protein phosphatases are associated with hepatic glycogen and microsomes, Biochim. Biophys. Acta 972, 221-231.
    • (1988) Biochim. Biophys. Acta , vol.972 , pp. 221-231
    • Schelling, D.1    Leader, D.P.2    Zammit, V.A.3    Cohen, P.4
  • 6
    • 0024261847 scopus 로고
    • The association of type 1. type 2A and type 2B phosphatases with the human T lymphocyte plasma membrane
    • Alexander, D. R., Hexham, J. M. & Crumpton, M. J. (1988) The association of type 1. type 2A and type 2B phosphatases with the human T lymphocyte plasma membrane, Biochem J. 256, 885-892.
    • (1988) Biochem J. , vol.256 , pp. 885-892
    • Alexander, D.R.1    Hexham, J.M.2    Crumpton, M.J.3
  • 7
    • 0020615499 scopus 로고
    • Separation and identification of type 1 and type 2 protein phosphatases from rabbit reticulocyte lysates
    • Foulkes, J. G., Ernst, V. & Levin, D. H. (1983) Separation and identification of type 1 and type 2 protein phosphatases from rabbit reticulocyte lysates, J. Biol. Chem. 258, 1439-1443.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1439-1443
    • Foulkes, J.G.1    Ernst, V.2    Levin, D.H.3
  • 8
    • 0029084967 scopus 로고
    • Interaction of the ribosomal protein. L5. with protein phosphatase type 1
    • Hirano, K., Ito, M. & Hartshorne, D. J. (1995) Interaction of the ribosomal protein. L5. with protein phosphatase type 1, J. Biol. Chem. 270, 19786-19790.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19786-19790
    • Hirano, K.1    Ito, M.2    Hartshorne, D.J.3
  • 9
    • 0026019658 scopus 로고
    • S. pombe sds22' essential for a midmitotic transition encodes a leucine-rich repeat protein that positiviely modulates protein phosphatase-1
    • Ohkura, H. & Yanagida, M. (1991) S. pombe sds22' essential for a midmitotic transition encodes a leucine-rich repeat protein that positiviely modulates protein phosphatase-1, Cell 64, 149-157.
    • (1991) Cell , vol.64 , pp. 149-157
    • Ohkura, H.1    Yanagida, M.2
  • 11
    • 0023780669 scopus 로고
    • Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase
    • DeGuzman, A. & Lee, E. Y. C. (1988) Preparation of low-molecular-weight forms of rabbit muscle protein phosphatase, Methods Enzymol. 159, 356-368.
    • (1988) Methods Enzymol. , vol.159 , pp. 356-368
    • DeGuzman, A.1    Lee, E.Y.C.2
  • 12
    • 0023644602 scopus 로고
    • The interrelationship between cAMP-dependent α and β subunit phosphorylation in the regulation of phosphorylase kinase activity. Studies using subunit specific phospliatases
    • Ramachandran, A., Goris, J., Waelkens, E., Merlevede, E. & Walsh. D. A. (1987) The interrelationship between cAMP-dependent α and β subunit phosphorylation in the regulation of phosphorylase kinase activity. Studies using subunit specific phospliatases. J. Biol. Chem. 262, 3210-3218.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3210-3218
    • Ramachandran, A.1    Goris, J.2    Waelkens, E.3    Merlevede, E.4    Walsh, D.A.5
  • 13
    • 0020540684 scopus 로고
    • 2+ /calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle
    • 2+ /calmodulin-dependent protein phosphatase (2B) from rabbit skeletal muscle, Eur. J. Biochem. 132, 289-295.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 289-295
    • Stewart, A.A.1    Ingebritsen, T.S.2    Cohen, P.3
  • 14
    • 0019890289 scopus 로고
    • A simplified procedure for the purification of the protein phosphatase modulator (inhibitor-2) from rabbit skeletal muscle
    • Yang, S.-D., Vandenheede, J. R. & Merlevede, W. (1981) A simplified procedure for the purification of the protein phosphatase modulator (inhibitor-2) from rabbit skeletal muscle, FEBS Lett. 132, 293-295.
    • (1981) FEBS Lett. , vol.132 , pp. 293-295
    • Yang, S.-D.1    Vandenheede, J.R.2    Merlevede, W.3
  • 15
    • 0002101212 scopus 로고
    • The isolation and crystallization of rabbit skeletal muscle phosphorylase b
    • Fischer, E. H. & Krebs, E. G. (1958) The isolation and crystallization of rabbit skeletal muscle phosphorylase b. J. Biol. Chem. 231, 65-71.
    • (1958) J. Biol. Chem. , vol.231 , pp. 65-71
    • Fischer, E.H.1    Krebs, E.G.2
  • 17
    • 0001303151 scopus 로고
    • Fractionnement préparatif des caséines de vache et de brebis pur Chromatographie sur D.E.A.E. cellulose en milieu urée et 2-mercaptoéthanol
    • Mercier, J. C., Maubois, J. L., Poznanski, S. & Ribadeau-Dumas, B. (1968) Fractionnement préparatif des caséines de vache et de brebis pur Chromatographie sur D.E.A.E. cellulose en milieu urée et 2-mercaptoéthanol, Bull. Soc. Chim. Biol. 50, 521-530.
    • (1968) Bull. Soc. Chim. Biol. , vol.50 , pp. 521-530
    • Mercier, J.C.1    Maubois, J.L.2    Poznanski, S.3    Ribadeau-Dumas, B.4
  • 18
    • 0024321507 scopus 로고
    • Purification of a hepatic S6 kinase from cycloheximide-treated rats
    • Price, D. J., Nemenoff, R. A. & Avruch, J. (1989) Purification of a hepatic S6 kinase from cycloheximide-treated rats. J. Biol. Chem. 264, 13825-13833.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13825-13833
    • Price, D.J.1    Nemenoff, R.A.2    Avruch, J.3
  • 19
    • 0024789526 scopus 로고
    • A stimulated S6 kinase from rat liver: Identity with the mitogen activated S6 kinase of 3T3 cells
    • Kozma, S. C., Lane, H. A., Ferrari, S., Luther, H., Siegmann, M. & Thomas, G. (1989) A stimulated S6 kinase from rat liver: identity with the mitogen activated S6 kinase of 3T3 cells, EMBO J. 8, 4125-4132.
    • (1989) EMBO J. , vol.8 , pp. 4125-4132
    • Kozma, S.C.1    Lane, H.A.2    Ferrari, S.3    Luther, H.4    Siegmann, M.5    Thomas, G.6
  • 20
    • 0017328441 scopus 로고
    • Comparison of the substrate specificities of protein phosphatases involved in the regulation of glycogen metabolism in rabbit skeletal muscle
    • Antoniw, J. F., Nimmo, H. G., Yeaman, S. J. & Cohen, P. (1977) Comparison of the substrate specificities of protein phosphatases involved in the regulation of glycogen metabolism in rabbit skeletal muscle, Biochem. J. 162, 423-433.
    • (1977) Biochem. J. , vol.162 , pp. 423-433
    • Antoniw, J.F.1    Nimmo, H.G.2    Yeaman, S.J.3    Cohen, P.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification 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
  • 22
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
    • Schägger, H. & von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa, Anal. Biochem 166, 368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 23
    • 0024262085 scopus 로고
    • Analysis of the 40S ribosomal protein S6 phosphorylation during the mitogenic response
    • Krieg, J., Olivier, A. R. & Thomas, G. (1988) Analysis of the 40S ribosomal protein S6 phosphorylation during the mitogenic response, Methods Enzymol. 164, 575-581.
    • (1988) Methods Enzymol. , vol.164 , pp. 575-581
    • Krieg, J.1    Olivier, A.R.2    Thomas, G.3
  • 25
    • 0025895035 scopus 로고
    • Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit
    • Kamibayashi, C., Estes, R., Slaughter, C. & Mumby, M. C. (1991) Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit. J. Biol. Chem. 266, 13251-13260.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13251-13260
    • Kamibayashi, C.1    Estes, R.2    Slaughter, C.3    Mumby, M.C.4
  • 26
    • 0029083171 scopus 로고
    • Subunit structure and regulation of protein phosphatase-1 in rat liver nuclei
    • Jagiello, I., Beullens, M., Stalmans, W. & Bollen, M. (1995) Subunit structure and regulation of protein phosphatase-1 in rat liver nuclei, J. Biol. Chem. 270, 17257-17263.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17257-17263
    • Jagiello, I.1    Beullens, M.2    Stalmans, W.3    Bollen, M.4
  • 27
    • 0023389116 scopus 로고
    • Chracterization of the catalytic subunits of the different types of polycation-stimulated protein phosphatases
    • Waelkens, E., Goris, J. & Merlevede, W. (1987) Chracterization of the catalytic subunits of the different types of polycation-stimulated protein phosphatases, Biochem. Int. 15, 385-393.
    • (1987) Biochem. Int. , vol.15 , pp. 385-393
    • Waelkens, E.1    Goris, J.2    Merlevede, W.3
  • 28
    • 0023881293 scopus 로고
    • Characterization of glycogen-synthase phosphutase and phosphorylase phosphatase in subcellular liver fractions
    • Bollen, M., Vandenheede, J. R., Goris, J. & Stalmans, W. (1988) Characterization of glycogen-synthase phosphutase and phosphorylase phosphatase in subcellular liver fractions, Biochem. Biophys. Acta 969, 66-77.
    • (1988) Biochem. Biophys. Acta , vol.969 , pp. 66-77
    • Bollen, M.1    Vandenheede, J.R.2    Goris, J.3    Stalmans, W.4
  • 29
    • 0026097955 scopus 로고
    • Purification and characterization of the glycogen-bound protein phosphatase from rat liver
    • Wera, S., Bollen, M. & Stalmans, W. (1991) Purification and characterization of the glycogen-bound protein phosphatase from rat liver, J. Biol. Chem. 260, 339-345.
    • (1991) J. Biol. Chem. , vol.260 , pp. 339-345
    • Wera, S.1    Bollen, M.2    Stalmans, W.3
  • 30
    • 0018368417 scopus 로고
    • The structure and function of eukaryotic ribosomes
    • Wool, I. G. (1979) The structure and function of eukaryotic ribosomes, Annu. Rev. Biochem. 48, 719-754.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 719-754
    • Wool, I.G.1
  • 31
    • 0021815656 scopus 로고
    • The protein phosphatases involved in cellular regulation. Influence of polyamines on the activities of protein phosphatase-1 and protein phosphatase-2A
    • Tung, H. Y. L., Pelech, S., Fisher, M. J., Pogson, C. I. & Cohen, P. (1985) The protein phosphatases involved in cellular regulation. Influence of polyamines on the activities of protein phosphatase-1 and protein phosphatase-2A, Eur. J. Biochem. 149, 305-313.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 305-313
    • Tung, H.Y.L.1    Pelech, S.2    Fisher, M.J.3    Pogson, C.I.4    Cohen, P.5
  • 33
    • 0027233603 scopus 로고
    • Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme
    • Alessi, D. R., Street, A. J., Cohen, P. & Cohen, P. T. W. (1993) Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme, Eur. J. Biochem 213, 1055-1066.
    • (1993) Eur. J. Biochem , vol.213 , pp. 1055-1066
    • Alessi, D.R.1    Street, A.J.2    Cohen, P.3    Cohen, P.T.W.4
  • 34
    • 0028143054 scopus 로고
    • Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed mutagenesis of inhibitor-2
    • Park, I.-K. & DePaoli-Roach, A. A. (1994) Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed mutagenesis of inhibitor-2, J. Biol. Chem. 269, 28919-28928.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28919-28928
    • Park, I.-K.1    DePaoli-Roach, A.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.