메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 793-798

Identification and characterization of three isotypes of protein phosphatase inhibitor-2 and their expression profiles during testis maturation in rats

Author keywords

cDNA cloning; Inhibitor 2; Protein phosphatase; Testis maturation

Indexed keywords

COMPLEMENTARY DNA; ENZYME INHIBITOR; MESSENGER RNA; PHOSPHOPROTEIN PHOSPHATASE;

EID: 0030425978     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0793r.x     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 0017240225 scopus 로고
    • A second heat-stable protein inhibitor of phosphorylase phosphatase from rabbit muscle
    • Huang, F. L. & Glinsmann, W. (1976) A second heat-stable protein inhibitor of phosphorylase phosphatase from rabbit muscle, FEBS Lett. 62, 326-329.
    • (1976) FEBS Lett. , vol.62 , pp. 326-329
    • Huang, F.L.1    Glinsmann, W.2
  • 3
    • 0028123476 scopus 로고
    • Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed imitagenesis of inhihitor-2
    • Park, I. K., Roach, P., Bondor, J., Fox, S. P. & DePaoli-Roach, A. A. (1994) Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed imitagenesis of inhihitor-2, J. Biol. Chem. 269, 944-954.
    • (1994) J. Biol. Chem. , vol.269 , pp. 944-954
    • Park, I.K.1    Roach, P.2    Bondor, J.3    Fox, S.P.4    DePaoli-Roach, A.A.5
  • 4
    • 0028347434 scopus 로고
    • Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E, coli
    • Helps, N. R., Street, A. J., Elledge, S. J. & Cohen, P. T. (1994) Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E, coli, FEBS Lett. 340, 93-98.
    • (1994) FEBS Lett. , vol.340 , pp. 93-98
    • Helps, N.R.1    Street, A.J.2    Elledge, S.J.3    Cohen, P.T.4
  • 6
    • 0027129777 scopus 로고
    • PCR cloning of the cDNA of rabbit skeletal muscle protein phosphatase inhibitor-2
    • Zhang, Z., Bai, G. & Lee, E. Y. (1992) PCR cloning of the cDNA of rabbit skeletal muscle protein phosphatase inhibitor-2, Biochem. Biophys. Res. Commun. 186, 1168-1170.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 1168-1170
    • Zhang, Z.1    Bai, G.2    Lee, E.Y.3
  • 7
    • 0028143054 scopus 로고
    • Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphalase
    • Park, I. K. & DePaoli-Roach, A. A. (1994) Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphalase, J. Biol. Chem. 269, 28919-28928.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28919-28928
    • Park, I.K.1    DePaoli-Roach, A.A.2
  • 8
    • 0017130995 scopus 로고
    • Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle
    • Huang, F. L. & Glinsmann, W. H. (1976) Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle, Eur. J. Biochem. 10, 419-426.
    • (1976) Eur. J. Biochem. , vol.10 , pp. 419-426
    • Huang, F.L.1    Glinsmann, W.H.2
  • 10
    • 0028360289 scopus 로고
    • Native cytosolic protein phosphatase-1 (PP-1S) containing modulator (inhibitor-2) is an active enzyme
    • Bollen, M., DePaoli-Roach, A. A. & Stalmans, W. (1994) Native cytosolic protein phosphatase-1 (PP-1S) containing modulator (inhibitor-2) is an active enzyme, FEBS Lett. 344, 196-200.
    • (1994) FEBS Lett. , vol.344 , pp. 196-200
    • Bollen, M.1    DePaoli-Roach, A.A.2    Stalmans, W.3
  • 11
    • 0026692912 scopus 로고
    • Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle
    • Gong, M. C., Cohen, P., Kitazawa, T., Ikebe, M., Musuo, M., Somlyo, A. P. & Somlyo, A. V. (1992) Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle, J. Biol. Chem. 267, 14662-14668.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Cohen, P.2    Kitazawa, T.3    Ikebe, M.4    Musuo, M.5    Somlyo, A.P.6    Somlyo, A.V.7
  • 12
    • 0021733910 scopus 로고
    • Amino acid sequence at the site on protein phosphatase inhihitor-2, phosphorylated by glycogen synthase kinase-3
    • Aitken, A., Holmes, C. F., Campbell, D. G., Resink, T. J., Cohen, P., Leung, C. T. & Williams, D. H. (1984) Amino acid sequence at the site on protein phosphatase inhihitor-2, phosphorylated by glycogen synthase kinase-3, Biochim. Biophys. Acta 790, 288-291.
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 288-291
    • Aitken, A.1    Holmes, C.F.2    Campbell, D.G.3    Resink, T.J.4    Cohen, P.5    Leung, C.T.6    Williams, D.H.7
  • 13
    • 0021162965 scopus 로고
    • Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase II (PC0.7)
    • DePaoli-Roach, A. A. (1984) Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase II (PC0.7), J. Biol. Chem. 259, 12 144-12 152.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12144-12152
    • DePaoli-Roach, A.A.1
  • 14
    • 0027957437 scopus 로고
    • Isoform differences in substrate recognition hy Glycogen synthase kinase 3a and 3b in the phosphorylation of phosphatase inhibitors
    • Wang, Q. M., Park, I.-K., Fiol, C. J., Roach, P. J. & DePaoli-Roach, A. A. (1994) Isoform differences in substrate recognition hy Glycogen synthase kinase 3a and 3b in the phosphorylation of phosphatase inhibitors, Biochemistry 33, 143-147.
    • (1994) Biochemistry , vol.33 , pp. 143-147
    • Wang, Q.M.1    Park, I.-K.2    Fiol, C.J.3    Roach, P.J.4    DePaoli-Roach, A.A.5
  • 15
    • 0021840722 scopus 로고
    • The protein phosphatases involved in cellular regulation: Purification and characterization of the glycogen-bound form of protein phophatase-1 from rat skeletal muscle
    • Stralfors, P., Hiraga, A. & Cohen, P. (1985) The protein phosphatases involved in cellular regulation: Purification and characterization of the glycogen-bound form of protein phophatase-1 from rat skeletal muscle, Eur. J. Biochem. 149, 295-303.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 295-303
    • Stralfors, P.1    Hiraga, A.2    Cohen, P.3
  • 16
    • 0024811049 scopus 로고
    • Regulation of protein phosphatase-1G from rabbit skeletal muscle
    • Hubbard, M. J. & Cohen, P. (1989) Regulation of protein phosphatase-1G from rabbit skeletal muscle, Eur. J. Biochem. 186, 711-716.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 711-716
    • Hubbard, M.J.1    Cohen, P.2
  • 17
    • 0025944344 scopus 로고
    • Molecular cloning and expression of the regulatory (RG1) subunit of the glycogen-associated protein phosphatase
    • Tang, P. M., Bondor, J. A., Swiderek, K. M. & DePaoli-Roach, A. A. (1991) Molecular cloning and expression of the regulatory (RG1) subunit of the glycogen-associated protein phosphatase, J. Biol. Chem. 266, 15 782-15 789.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15782-15789
    • Tang, P.M.1    Bondor, J.A.2    Swiderek, K.M.3    DePaoli-Roach, A.A.4
  • 18
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits: The major myosin phophatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi, D. R., MacDougall, L. K., Sola, M. M., Ikebe, M. & Cohen, P. (1992) The control of protein phosphatase-1 by targetting subunits: The major myosin phophatase in avian smooth muscle is a novel form of protein phosphatase-1, Eur. J. Biochem. 210, 1023-1035.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.R.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 19
    • 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. (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.4
  • 20
    • 0025098525 scopus 로고
    • Cell cycle oscillation of phosphatase inhibitor-2 in rat fibroblasts coincident with p34cdc2 restriction
    • Brautigan, D. L., Sunwoo, J., Labbe, J. C., Fernandez, A. & Lamb, N. J. (1990) Cell cycle oscillation of phosphatase inhibitor-2 in rat fibroblasts coincident with p34cdc2 restriction, Nature 344, 74-78.
    • (1990) Nature , vol.344 , pp. 74-78
    • Brautigan, D.L.1    Sunwoo, J.2    Labbe, J.C.3    Fernandez, A.4    Lamb, N.J.5
  • 21
    • 0021381028 scopus 로고
    • A technique for radio labeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P. & Vogelstein, B. (1984) A technique for radio labeling DNA restriction endonuclease fragments to high specific activity, Anal. Biochem. 137, 266-267.
    • (1984) Anal. Biochem. , vol.137 , pp. 266-267
    • Feinberg, A.P.1    Vogelstein, B.2
  • 22
    • 0024284551 scopus 로고
    • Lambda ZAP: A bacteriophage lambda expression vector with in vivo excision properties
    • Short, J. M., Fernandez, J. M., Sorge, J. A. & Huse, W. D. (1988) Lambda ZAP: a bacteriophage lambda expression vector with in vivo excision properties, Nucleic Acids Res. 16, 7583-7600.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7583-7600
    • Short, J.M.1    Fernandez, J.M.2    Sorge, J.A.3    Huse, W.D.4
  • 23
    • 0001939094 scopus 로고
    • RACE: Rapid Amplification of cDNA Ends
    • (Innis, M., Gelfand, D. H., Sninsky, J. J. & White, T. J., eds) Academic Press, Inc., San Diego
    • Frohman, M. A. (1990) RACE: Rapid Amplification of cDNA Ends. in PCR protocols (Innis, M., Gelfand, D. H., Sninsky, J. J. & White, T. J., eds) Academic Press, Inc., San Diego
    • (1990) PCR Protocols
    • Frohman, M.A.1
  • 25
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. & Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 27
    • 0001057395 scopus 로고
    • Assay and purification of protein (serine/ threonine) phosphatases
    • (Hardie, D. G., ed.) Oxford Univ. Press., Oxford
    • MacKintosh, C. (1993) Assay and purification of protein (serine/ threonine) phosphatases, in Protein phosphorylation (Hardie, D. G., ed.) pp. 197-230, Oxford Univ. Press., Oxford.
    • (1993) Protein Phosphorylation , pp. 197-230
    • MacKintosh, C.1
  • 29
    • 0029002733 scopus 로고
    • Molecular cloning of the cDNA for rat phosphatase inhibitor-2 and its wide gene expression in the central nervous system
    • Sakagami, H. & Kondo, H. (1995) Molecular cloning of the cDNA for rat phosphatase inhibitor-2 and its wide gene expression in the central nervous system, J. Chem. Neuroanat. 8, 259-266.
    • (1995) J. Chem. Neuroanat. , vol.8 , pp. 259-266
    • Sakagami, H.1    Kondo, H.2
  • 30
    • 0021770224 scopus 로고
    • Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs
    • Kozak, M. (1984) Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs, Nucleic Acids Res. 12, 857-872.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 857-872
    • Kozak, M.1
  • 31
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G. & Kamen, R. (1986) A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation, Cell 46, 659-667.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 32
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Roger, S., Wells, R. & Rechsteiner, M. (1986) Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis, Science 234, 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Roger, S.1    Wells, R.2    Rechsteiner, M.3
  • 33
    • 0023151001 scopus 로고
    • Do myc, fos and E1A function as protein phosphatase inhibitor?
    • Rechsteiner, M. (1987) Do myc, fos and E1A function as protein phosphatase inhibitor? Biochem. Biophys. Res. Commun. 143, 194-198.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 194-198
    • Rechsteiner, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.