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Volumn 115, Issue 19, 2002, Pages 3739-3745

Domains of type 1 protein phosphatase inhibitor-2 required for nuclear and cytoplasmic localization in response to cell-cell contact

Author keywords

Cell density; Green fluorescent protein; Nuclear import

Indexed keywords

GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR 2; UNCLASSIFIED DRUG;

EID: 0036798297     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00052     Document Type: Article
Times cited : (14)

References (26)
  • 1
    • 0035901937 scopus 로고    scopus 로고
    • Tumor suppressor protein VHL is induced at high cell density and mediates contact inhibition of cell growth
    • Baba, M., Hirai, S., Kawakami, S., Kishida, T., Sakai, N., Kaneko, S., Yao, M., Shuin, T., Kubota, Y., Hosaka, M. et al. (2001). Tumor suppressor protein VHL is induced at high cell density and mediates contact inhibition of cell growth. Oncogene J. 20, 2727-2736.
    • (2001) Oncogene J , vol.20 , pp. 2727-2736
    • Baba, M.1    Hirai, S.2    Kawakami, S.3    Kishida, T.4    Sakai, N.5    Kaneko, S.6    Yao, M.7    Shuin, T.8    Kubota, Y.9    Hosaka, M.10
  • 2
    • 0035399464 scopus 로고    scopus 로고
    • Combinatorial control of protein phosphatase-1
    • Bollen, M. (2001). Combinatorial control of protein phosphatase-1. Trends Biochem. Sci. 26, 426-431.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 426-431
    • Bollen, M.1
  • 5
    • 0028040192 scopus 로고
    • Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae
    • Cannon, J. F., Pringle, J. R., Fiechter, A. and Khalil, M. (1994). Characterization of glycogen-deficient glc mutants of Saccharomyces cerevisiae. Genetics J. 136, 485-503.
    • (1994) Genetics J , vol.136 , pp. 485-503
    • Cannon, J.F.1    Pringle, J.R.2    Fiechter, A.3    Khalil, M.4
  • 6
    • 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
  • 7
    • 17544377868 scopus 로고    scopus 로고
    • Dephosphorylation of Sp1 by protein phosphatase 1 is involved in the glucose-mediated activation of the acetyl-CoA carboxylase gene
    • Daniel, S., Zhang, S., DePaoli-Roach, A. A. and Kim, K. H. (1996). Dephosphorylation of Sp1 by protein phosphatase 1 is involved in the glucose-mediated activation of the acetyl-CoA carboxylase gene. J. Biol. Chem. 271, 14692-14697.
    • (1996) J. Biol. Chem , vol.271 , pp. 14692-14697
    • Daniel, S.1    Zhang, S.2    DePaoli-Roach, A.A.3    Kim, K.H.4
  • 8
    • 0030977268 scopus 로고    scopus 로고
    • Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1
    • Egloff, M., Johnson, D. F., Moorhead, G., Cohen, P. T. W., Cohen, P. and Barford, D. (1997). Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16, 1876-1887.
    • (1997) EMBO J , vol.16 , pp. 1876-1887
    • Egloff, M.1    Johnson, D.F.2    Moorhead, G.3    Cohen, P.T.W.4    Cohen, P.5    Barford, D.6
  • 9
    • 0029121296 scopus 로고
    • Nuclear export signals and the fast track to the cytoplasm
    • Gerace, L. (1995). Nuclear export signals and the fast track to the cytoplasm. Cell 82, 341-344.
    • (1995) Cell , vol.82 , pp. 341-344
    • Gerace, L.1
  • 10
    • 0033405538 scopus 로고    scopus 로고
    • Drosophila melanogaster protein phosphatase inhibitor-2: Identification of a site important for PP1 inhibition
    • Helps, N. R. and Cohen, P. T. W. (1999). Drosophila melanogaster protein phosphatase inhibitor-2: identification of a site important for PP1 inhibition. FEBS Lett. 463, 72-76.
    • (1999) FEBS Lett , vol.463 , pp. 72-76
    • Helps, N.R.1    Cohen, P.T.W.2
  • 11
    • 0017130995 scopus 로고
    • Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle
    • Huang, F. L. and Glinsmann, W. H. (1976). Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle. Euro. J. Biochem. 70, 419-426.
    • (1976) Euro. J. Biochem , vol.70 , pp. 419-426
    • Huang, F.L.1    Glinsmann, W.H.2
  • 13
    • 0031434815 scopus 로고    scopus 로고
    • Multisite phosphorylation and the nuclear localization of phosphatase inhibitor 2-green fluorescent protein (Inh2-GFP) fusion protein during S phase of the cell growth cycle
    • Kakinoki, Y., Somers, J. and Brautigan, D. L. (1997). Multisite phosphorylation and the nuclear localization of phosphatase inhibitor 2-green fluorescent protein (Inh2-GFP) fusion protein during S phase of the cell growth cycle. J. Biol. Chem. 272, 32308-32314.
    • (1997) J. Biol. Chem , vol.272 , pp. 32308-32314
    • Kakinoki, Y.1    Somers, J.2    Brautigan, D.L.3
  • 14
    • 0030425978 scopus 로고    scopus 로고
    • Identification and characterization of three isotypes, of protein phosphatase inhibitor-2 and their expression profiles during testis maturation in rats
    • Osawa, Y., Nakagama, H., Shima, H., Sugimau, T. and Nagao, M. (1996). Identification and characterization of three isotypes, of protein phosphatase inhibitor-2 and their expression profiles during testis maturation in rats. Eur. J. Biochem. 242, 793-798.
    • (1996) Eur. J. Biochem , vol.242 , pp. 793-798
    • Osawa, Y.1    Nakagama, H.2    Shima, H.3    Sugimau, T.4    Nagao, M.5
  • 15
    • 0035193242 scopus 로고    scopus 로고
    • Nuclear transport mechanisms
    • Quimby, B. B. and Corbett, A. H. (2001). Nuclear transport mechanisms. Cell. Mol. Life Sci. 58, 1766-1773.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1766-1773
    • Quimby, B.B.1    Corbett, A.H.2
  • 16
    • 0021104279 scopus 로고
    • Characterization of a reconstituted Mg-ATP-dependent phosphatase
    • Resink, T. J., Hemmings, B. A., Tung, H. Y. L. and Cohen, P. (1983). Characterization of a reconstituted Mg-ATP-dependent phosphatase. Eur. J. Biochem. 133, 455-461.
    • (1983) Eur. J. Biochem , vol.133 , pp. 455-461
    • Resink, T.J.1    Hemmings, B.A.2    Tung, H.Y.L.3    Cohen, P.4
  • 19
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases - New avenues for cell regulation
    • Shenolikar, S. (1994). Protein serine/threonine phosphatases - new avenues for cell regulation. Annu. Rev. Cell Biol. 10, 55-86.
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 20
    • 0021840722 scopus 로고
    • The protein phosphatases; involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle
    • Strålfors, P., Hiraga, A. and Cohen, P. (1985). The protein phosphatases; involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle. Eur. J. Biochem. 149, 295-303.
    • (1985) Eur. J. Biochem , vol.149 , pp. 295-303
    • Strålfors, P.1    Hiraga, A.2    Cohen, P.3
  • 22
    • 0030059623 scopus 로고    scopus 로고
    • Variable nuclear cytoplasmic distribution of the 11.5 kDa zinc-binding protein (parathymosin-alpha) and identification of a bipartite nuclear localization signal
    • Trompeter, H.-L., Brankd, I. A. and Soling, H.-D. (1996). Variable nuclear cytoplasmic distribution of the 11.5 kDa zinc-binding protein (parathymosin-alpha) and identification of a bipartite nuclear localization signal. J. Biol. Chem. 271, 1187-1193.
    • (1996) J. Biol. Chem , vol.271 , pp. 1187-1193
    • Trompeter, H.-L.1    Brankd, I.A.2    Soling, H.-D.3
  • 23
    • 0027880143 scopus 로고
    • Cell density modulates growth, extracellular matrix, and protein synthesis of cultured rat mesangial cells
    • Wolthuis, A., Boes, A. and Grond, J. (1993). Cell density modulates growth, extracellular matrix, and protein synthesis of cultured rat mesangial cells. Am. J. Pathol. 143, 1209-1219.
    • (1993) Am. J. Pathol , vol.143 , pp. 1209-1219
    • Wolthuis, A.1    Boes, A.2    Grond, J.3
  • 24
    • 0034725628 scopus 로고    scopus 로고
    • Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase
    • Yang, J., Hurley, T. D. and DePaoli-Roach, A. (2000). Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. J. Biol. Chem. 275, 22635-22644.
    • (2000) J. Biol. Chem , vol.275 , pp. 22635-22644
    • Yang, J.1    Hurley, T.D.2    DePaoli-Roach, A.3
  • 25
    • 0019888478 scopus 로고
    • Identification of inhibitor-2 as the ATP-Mg-dependent protein phosphatase modulator
    • Yang, S.-D., Vandenheede, J. R. and Merlevede, W. (1981). Identification of inhibitor-2 as the ATP-Mg-dependent protein phosphatase modulator. J. Biol. Chem. 256, 10231-10234.
    • (1981) J. Biol. Chem , vol.256 , pp. 10231-10234
    • Yang, S.-D.1    Vandenheede, J.R.2    Merlevede, W.3
  • 26
    • 0027129777 scopus 로고
    • PCR cloning of the cDNA of rabbit skeletal muscle protein phosphatase inhibitor-2
    • Zhang, Z., Bai, G. and Lee, E. Y. C. (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.C.3


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