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Volumn 10, Issue 6, 1999, Pages 1997-2015

Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55

Author keywords

[No Author keywords available]

Indexed keywords

OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN SUBUNIT; TAUTOMYCIN; VIMENTIN;

EID: 0032978487     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.6.1997     Document Type: Article
Times cited : (94)

References (70)
  • 1
    • 0023127372 scopus 로고
    • Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and Mg-ATP-dependent phosphorylase phosphatases
    • Agostinis, P., Goris, J., Waelkens, E., Pinna, L.A., Marchiori, F., and Merlevede, W. (1987). Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and Mg-ATP-dependent phosphorylase phosphatases. J. Biol. Chem. 262, 1060-1064.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1060-1064
    • Agostinis, P.1    Goris, J.2    Waelkens, E.3    Pinna, L.A.4    Marchiori, F.5    Merlevede, W.6
  • 3
    • 0030466725 scopus 로고    scopus 로고
    • The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1
    • Andjelkovic, N., Zolnierowicz, S., Van-Hoof, C., Goris, J., and Hemmings, B.A. (1996). The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15, 7156-7167.
    • (1996) EMBO J. , vol.15 , pp. 7156-7167
    • Andjelkovic, N.1    Zolnierowicz, S.2    Van-Hoof, C.3    Goris, J.4    Hemmings, B.A.5
  • 4
    • 0000290454 scopus 로고
    • Quantitative electrophoresis in polyacrylamide gels of 2-40%
    • Blattler, D.P., Garner, F., Van Slyke, K., and Bradley, A. (1972). Quantitative electrophoresis in polyacrylamide gels of 2-40%. J. Chromatogr. 64, 147-155.
    • (1972) J. Chromatogr. , vol.64 , pp. 147-155
    • Blattler, D.P.1    Garner, F.2    Van Slyke, K.3    Bradley, A.4
  • 5
    • 0021352916 scopus 로고
    • 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin
    • Blose, S.H., Meltzer, D.I., and Feramisco, J.R. (1984). 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin. J. Cell Biol. 98, 847-858.
    • (1984) J. Cell Biol. , vol.98 , pp. 847-858
    • Blose, S.H.1    Meltzer, D.I.2    Feramisco, J.R.3
  • 6
    • 0027522757 scopus 로고
    • PPX, a novel protein serine/threonine phosphatase localized to centrosomes
    • Brewis, N.D., Street, A.J., Prescott, A.R., and Cohen, P.T. (1993). PPX, a novel protein serine/threonine phosphatase localized to centrosomes. EMBO J. 12, 987-996.
    • (1993) EMBO J. , vol.12 , pp. 987-996
    • Brewis, N.D.1    Street, A.J.2    Prescott, A.R.3    Cohen, P.T.4
  • 7
    • 0028276611 scopus 로고
    • Different oligomeric forms of protein phosphatase 2A activate and inhibit SV40 DNA replication
    • Cegielska, A., Shaffer, S., Derua, R., Goris, J., and Virshup, D.M. (1994). Different oligomeric forms of protein phosphatase 2A activate and inhibit SV40 DNA replication. Mol. Cell. Biol. 14, 4616-4623.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4616-4623
    • Cegielska, A.1    Shaffer, S.2    Derua, R.3    Goris, J.4    Virshup, D.M.5
  • 8
    • 0023711798 scopus 로고
    • Calcium phosphate-mediated gene transfer: A highly efficient transfection system for stably transforming cells with plasmid DNA
    • Chen, C.A., and Okayama, H. (1988). Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. Biotechniques 6, 632-638.
    • (1988) Biotechniques , vol.6 , pp. 632-638
    • Chen, C.A.1    Okayama, H.2
  • 9
    • 0028133445 scopus 로고
    • A novel protein human serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus
    • Chen, M.X., McPartlin, A. E., Brown, L., Chen, Y.H., Barker, H.M., and Cohen, P.T. (1994). A novel protein human serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J. 15, 4278-4290.
    • (1994) EMBO J. , vol.15 , pp. 4278-4290
    • Chen, M.X.1    McPartlin, A.E.2    Brown, L.3    Chen, Y.H.4    Barker, H.M.5    Cohen, P.T.6
  • 10
    • 0025872907 scopus 로고
    • Phorbol acetate enhances the phosphorylation of cytokeratins 8 an 18 in human colonic epithelial cells
    • Chou, C-F., and Omary, M.B. (1991). Phorbol acetate enhances the phosphorylation of cytokeratins 8 an 18 in human colonic epithelial cells. FEBS Lett. 282, 200-204.
    • (1991) FEBS Lett. , vol.282 , pp. 200-204
    • Chou, C.-F.1    Omary, M.B.2
  • 11
    • 0025130177 scopus 로고
    • Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin
    • Chou, Y.-H., Bischoff, J.R., Beach, D., and Goldman, R.D. (1990). Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin. Cell 62, 1063-1071.
    • (1990) Cell , vol.62 , pp. 1063-1071
    • Chou, Y.-H.1    Bischoff, J.R.2    Beach, D.3    Goldman, R.D.4
  • 12
    • 0022413059 scopus 로고
    • Regulation of protein phosphorylation of the intermediate-sized filament vimentin in cilary epithelium of the mammalian eye
    • Coca-Prados, M. (1985). Regulation of protein phosphorylation of the intermediate-sized filament vimentin in cilary epithelium of the mammalian eye. J. Biol. Chem. 260, 10332-10338.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10332-10338
    • Coca-Prados, M.1
  • 14
    • 0027436764 scopus 로고
    • Role of phosphorylation in keratin and vimentin filament integrity in cultured thyroid epithelial cells
    • Deery, W.J. (1993). Role of phosphorylation in keratin and vimentin filament integrity in cultured thyroid epithelial cells. Cell Motil. Cytoskeleton 26, 325-339.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 325-339
    • Deery, W.J.1
  • 15
    • 0020403113 scopus 로고
    • Hormonal regulation of protein synthesis, secretion and phosphorylation in cultured rat Sertoli cells
    • DePhilip, R.M., and Kierszenbaum, A.L. (1982). Hormonal regulation of protein synthesis, secretion and phosphorylation in cultured rat Sertoli cells. Proc. Natl. Acad. Sci. USA 79, 6551-6555.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6551-6555
    • Dephilip, R.M.1    Kierszenbaum, A.L.2
  • 16
    • 0022494971 scopus 로고
    • Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
    • Ellis, L., Clauser, E., Morgan, D.O., Edery, M., Roth, R., and Rutter, W.J. (1986). Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45, 721-732.
    • (1986) Cell , vol.45 , pp. 721-732
    • Ellis, L.1    Clauser, E.2    Morgan, D.O.3    Edery, M.4    Roth, R.5    Rutter, W.J.6
  • 18
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • Favre, B., Turowski, P., and Hemmings, B.A. (1997). Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. J. Biol. Chem. 272, 13856-13863.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 19
    • 0028361380 scopus 로고
    • The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo
    • Favre, B., Zolnierowicz, S., Turowski, P., and Hemmings, B.A. (1994). The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. J. Biol. Chem. 269, 16311-16317.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16311-16317
    • Favre, B.1    Zolnierowicz, S.2    Turowski, P.3    Hemmings, B.A.4
  • 20
    • 0026561879 scopus 로고
    • Protein phosphatase type 1 in mammalian cell mitosis: Chromosomal localization and involvement in mitotic exit
    • Fernandez, A., Brautigan, D.L., and Lamb, N.J.C. (1992). Protein phosphatase type 1 in mammalian cell mitosis: chromosomal localization and involvement in mitotic exit. J. Cell Biol. 116, 1421-1430.
    • (1992) J. Cell Biol. , vol.116 , pp. 1421-1430
    • Fernandez, A.1    Brautigan, D.L.2    Lamb, N.J.C.3
  • 21
    • 0025363197 scopus 로고
    • Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells
    • Fernandez, A., Brautigan, D.L., Mumby, M., and Lamb, N.J.C. (1990). Protein phosphatase type-1, not type-2A, modulates actin microfilament integrity and myosin light chain phosphorylation in living nonmuscle cells. J. Cell Biol. 111, 103-112.
    • (1990) J. Cell Biol. , vol.111 , pp. 103-112
    • Fernandez, A.1    Brautigan, D.L.2    Mumby, M.3    Lamb, N.J.C.4
  • 22
    • 0027337563 scopus 로고
    • 1 is the major enzyme in vertebrate cell extracts that dephosphorylates several physiological substrates for cyclin-dependent protein kinases
    • 1 is the major enzyme in vertebrate cell extracts that dephosphorylates several physiological substrates for cyclin-dependent protein kinases. Mol. Biol. Cell 4, 669-677.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 669-677
    • Ferrigno, P.1    Langan, T.A.2    Cohen, P.3
  • 23
    • 0018128026 scopus 로고
    • Antibody to prekeratin: Decoration of tonofilament-like arrays in various cells of epithelial character
    • Franke, W.W., Weber, K., Osborn, M., Schmid, E., and Freudenstein, C. (1978). Antibody to prekeratin: decoration of tonofilament-like arrays in various cells of epithelial character. Exp. Cell Res. 116, 429-445.
    • (1978) Exp. Cell Res. , vol.116 , pp. 429-445
    • Franke, W.W.1    Weber, K.2    Osborn, M.3    Schmid, E.4    Freudenstein, C.5
  • 24
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function and disease
    • Fuchs, E., and Weber, K. (1994). Intermediate filaments: structure, dynamics, function and disease. Annu. Rev. Biochem. 63, 345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 25
    • 0026709066 scopus 로고
    • cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells
    • Girard, F., Strausfeld, U., Cavadore, J.-C., Russel, P., Fernandez, A., and Lamb, N.J.C. (1992). cdc25 is a nuclear protein expressed constitutively throughout the cell cycle in nontransformed mammalian cells. J. Cell Biol. 118, 785-794.
    • (1992) J. Cell Biol. , vol.118 , pp. 785-794
    • Girard, F.1    Strausfeld, U.2    Cavadore, J.-C.3    Russel, P.4    Fernandez, A.5    Lamb, N.J.C.6
  • 26
    • 0030475207 scopus 로고    scopus 로고
    • 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Cα correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer
    • Hansra, G., Bornancin, F., Whelan, R., Hemmings, B.A., and Parker, P.J. (1996). 12-O-Tetradecanoylphorbol-13-acetate-induced dephosphorylation of protein kinase Cα correlates with the presence of a membrane-associated protein phosphatase 2A heterotrimer. J. Biol. Chem. 271, 32785-32788.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32785-32788
    • Hansra, G.1    Bornancin, F.2    Whelan, R.3    Hemmings, B.A.4    Parker, P.J.5
  • 27
    • 0024592297 scopus 로고
    • Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism
    • Haystead, T.A., Sim, A.T., Carling, D., Honnor, R.C., Tsukitani, Y., Cohen, P., and Hardie, D.G. (1989). Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism. Nature 337, 78-81.
    • (1989) Nature , vol.337 , pp. 78-81
    • Haystead, T.A.1    Sim, A.T.2    Carling, D.3    Honnor, R.C.4    Tsukitani, Y.5    Cohen, P.6    Hardie, D.G.7
  • 28
    • 0026091769 scopus 로고
    • CDC55, a Sacchawmyces cerevisiae gene involved in cellular morphogenesis: Identification, characterization, and homology to the b subunit of mammalian type 2A protein phosphatase
    • Healy, A.M., Zolnierowicz, S., Stapleton, A.E., Goebl, M., DePaoli-Roach, A.A., and Pringle, J.R. (1991). CDC55, a Sacchawmyces cerevisiae gene involved in cellular morphogenesis: identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase. Mol. Cell. Biol. 11, 5767-5780.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5767-5780
    • Healy, A.M.1    Zolnierowicz, S.2    Stapleton, A.E.3    Goebl, M.4    DePaoli-Roach, A.A.5    Pringle, J.R.6
  • 31
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard, M.J., and 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
  • 33
    • 0028021165 scopus 로고
    • Comparison of heterotrimeric protein phosphatase 2A containing different B subunits
    • Kamibayashi, C., Estes, R., Lickteig, R.L., Yang, S.-I., Craft, C., and Mumby, M.C. (1994). Comparison of heterotrimeric protein phosphatase 2A containing different B subunits. J. Biol. Chem. 269, 20139-20148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20139-20148
    • Kamibayashi, C.1    Estes, R.2    Lickteig, R.L.3    Yang, S.-I.4    Craft, C.5    Mumby, M.C.6
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0027435152 scopus 로고
    • Vimentin serves as a phosphatase sink during the apparent activation of protein kinases by okadaic acid in mammalian cells
    • Lai, Y.K., Lee, W.C., and Chen, K.-D. (1993). Vimentin serves as a phosphatase Sink During the apparent activation of protein kinases by okadaic acid in mammalian cells. J. Cell. Biochem. 53, 161-168.
    • (1993) J. Cell. Biochem. , vol.53 , pp. 161-168
    • Lai, Y.K.1    Lee, W.C.2    Chen, K.-D.3
  • 36
    • 0030842531 scopus 로고    scopus 로고
    • Microinjection of antibodies into mammalian cells
    • Lamb, N.J.C., and Fernandez, A. (1997). Microinjection of antibodies into mammalian cells. Methods Enzymol. 283, 72-83.
    • (1997) Methods Enzymol. , vol.283 , pp. 72-83
    • Lamb, N.J.C.1    Fernandez, A.2
  • 37
    • 0024328163 scopus 로고
    • Modulation of vimentin containing intermediate filament distribution and phosphorylation in living fibroblasts by the cAMP-dependent protein kinase
    • Lamb, N.J.C., Fernandez, A., Feramisco, J.R., and Welch, W.J. (1989). Modulation of vimentin containing intermediate filament distribution and phosphorylation in living fibroblasts by the cAMP-dependent protein kinase. J. Cell Biol. 108, 2409-2422.
    • (1989) J. Cell Biol. , vol.108 , pp. 2409-2422
    • Lamb, N.J.C.1    Fernandez, A.2    Feramisco, J.R.3    Welch, W.J.4
  • 38
    • 0028348011 scopus 로고
    • Inhibition of cdc2 activation by INH/PP2A
    • Lee, T.H., Turck, C., and Kirschner, M.W. (1994). Inhibition of cdc2 activation by INH/PP2A. Mol. Biol. Cell 5, 323-338.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 323-338
    • Lee, T.H.1    Turck, C.2    Kirschner, M.W.3
  • 39
    • 0026613093 scopus 로고
    • Reversible hyperphosphorylation and reorganization of vimentin intermediate filaments by okadaic acid in 9L rat brain tumor cells
    • Lee, W.C., Yu, J.S., Yang, S.D., and Lai, Y.K. (1992). Reversible hyperphosphorylation and reorganization of vimentin intermediate filaments by okadaic acid in 9L rat brain tumor cells. J. Cell. Biochem. 49, 378-393.
    • (1992) J. Cell. Biochem. , vol.49 , pp. 378-393
    • Lee, W.C.1    Yu, J.S.2    Yang, S.D.3    Lai, Y.K.4
  • 43
    • 0028359957 scopus 로고
    • Protein phosphatase 2A - A "menage a trois."
    • Mayer-Jaekel, R.E., and Hemmings, B.A. (1994). Protein phosphatase 2A - a "menage a trois." Trends Cell Biol. 4, 287-291.
    • (1994) Trends Cell Biol. , vol.4 , pp. 287-291
    • Mayer-Jaekel, R.E.1    Hemmings, B.A.2
  • 44
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright, B., Rivers, A.M., Audlin, S., and Virshup, D.M. (1996). The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J. Biol. Chem. 271, 22081-22089.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 45
    • 0028832251 scopus 로고
    • Identification of a new family of protein phosphatase 2A regulatory subunits
    • McCright, B., and Virshup, D.M. (1995). Identification of a new family of protein phosphatase 2A regulatory subunits. J. Biol. Chem. 270, 26123-26128.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26123-26128
    • McCright, B.1    Virshup, D.M.2
  • 46
    • 0029669963 scopus 로고    scopus 로고
    • Site-specific dephosphorylation of tau protein at Ser202/Thr205 in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A
    • Merrick, S.E., Demoise, D.C., and Lee V.M. (1996). Site-specific dephosphorylation of tau protein at Ser202/Thr205 in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A. J. Biol. Chem. 271, 5589-5594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5589-5594
    • Merrick, S.E.1    Demoise, D.C.2    Lee, V.M.3
  • 48
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P.H. (1975). High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 49
    • 0026512195 scopus 로고
    • The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36-and 63-kilodalton PP2A subunits, bears little resemblance to T antigens
    • Pallas, D.C., Weller, W., Jaspers, S., Miller, T.B., Lane, W.S., and Roberts, T.M. (1992). The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton protein which is apparently substituted for by T antigens in complexes with the 36-and 63-kilodalton PP2A subunits, bears little resemblance to T antigens. J. Virol. 66, 886-893.
    • (1992) J. Virol. , vol.66 , pp. 886-893
    • Pallas, D.C.1    Weller, W.2    Jaspers, S.3    Miller, T.B.4    Lane, W.S.5    Roberts, T.M.6
  • 50
    • 0029160524 scopus 로고
    • The G-protein-coupled receptor phosphatase: A protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity
    • Pitcher, J.A., Payne, E.S., Csortos, C., DePaoli-Roach, A.A., and Lefkowitz, R.J. (1995). The G-protein-coupled receptor phosphatase: a protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity. Proc. Natl. Acad. Sci. USA 92, 8343-8347.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8343-8347
    • Pitcher, J.A.1    Payne, E.S.2    Csortos, C.3    DePaoli-Roach, A.A.4    Lefkowitz, R.J.5
  • 51
    • 0029018031 scopus 로고
    • Neurofilament-associated protein phosphatase 2A: Its possible role in preserving neurofilaments in filamentous states
    • Saito, T., Shima, H., Osawa, Y., Nagao, M., Hemmings, B.A., Kishimoto, T., and Hisanaga, S. (1995). Neurofilament-associated protein phosphatase 2A: its possible role in preserving neurofilaments in filamentous states. Biochemistry 34, 7376-7384.
    • (1995) Biochemistry , vol.34 , pp. 7376-7384
    • Saito, T.1    Shima, H.2    Osawa, Y.3    Nagao, M.4    Hemmings, B.A.5    Kishimoto, T.6    Hisanaga, S.7
  • 53
    • 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
  • 54
    • 0028360550 scopus 로고
    • Alternative cell fate choice induced by low-level expression of a regulator of protein phosphatase 2A in the Drosophila peripheral nervous system
    • Shiomi, K., Takeichi, M., Nishida, Y., Nishi, Y., and Uemura, T. (1994). Alternative cell fate choice induced by low-level expression of a regulator of protein phosphatase 2A in the Drosophila peripheral nervous system. Development 120, 1591-1599.
    • (1994) Development , vol.120 , pp. 1591-1599
    • Shiomi, K.1    Takeichi, M.2    Nishida, Y.3    Nishi, Y.4    Uemura, T.5
  • 55
    • 0028924295 scopus 로고
    • A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle
    • Sontag, E., Nunbhakdi-Craig, V., Bloom, G.S., and Mumby, M.C. (1995). A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J. Cell Biol. 128, 1131-1144.
    • (1995) J. Cell Biol. , vol.128 , pp. 1131-1144
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Bloom, G.S.3    Mumby, M.C.4
  • 56
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of tau by protein phosphatase 2A
    • Sontag, E., Nunbhakdi-Craig, V., Lee, G., Bloom, G.S., and Mumby, M.C. (1996). Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron 17, 1201-1207.
    • (1996) Neuron , vol.17 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 57
    • 0023658640 scopus 로고
    • Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A
    • Stone, S.R., Hofsteenge, J., and Hemmings, B.A. (1987). Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A. Biochemistry 26, 7215-7220.
    • (1987) Biochemistry , vol.26 , pp. 7215-7220
    • Stone, S.R.1    Hofsteenge, J.2    Hemmings, B.A.3
  • 58
    • 0001962451 scopus 로고
    • A manual of methods for baculovirus vectors and insect cell culture procedures
    • Summers, M.D., and Smith, G.E. (1987). A manual of methods for baculovirus vectors and insect cell culture procedures. Tex. Agric. Exp. Stn. Bull. 1555, 1-57.
    • (1987) Tex. Agric. Exp. Stn. Bull. , vol.1555 , pp. 1-57
    • Summers, M.D.1    Smith, G.E.2
  • 60
    • 0029915709 scopus 로고    scopus 로고
    • Identification of a novel protein phosphatase 2A regulatory subunit highly expressed in muscle
    • Tehrani, M.A., Mumby, M.C., and Kamibayashi, C. (1996). Identification of a novel protein phosphatase 2A regulatory subunit highly expressed in muscle. J. Biol. Chem. 271, 5164-5170.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5164-5170
    • Tehrani, M.A.1    Mumby, M.C.2    Kamibayashi, C.3
  • 61
    • 0030874269 scopus 로고    scopus 로고
    • Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65α
    • Turowski, P., Favre, B., Campbell, K.S., Lamb, N.J.C., and Hemmings, B.A. (1997). Modulation of the enzymatic properties of protein phosphatase 2A catalytic subunit by the recombinant 65-kDa regulatory subunit PR65α. Eur. J. Biochem. 248, 200-208.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 200-208
    • Turowski, P.1    Favre, B.2    Campbell, K.S.3    Lamb, N.J.C.4    Hemmings, B.A.5
  • 62
    • 0028940016 scopus 로고
    • Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression
    • Turowski, P., Fernandez, A., Favre, B., Lamb, N.J.C., and Hemmings, B.A. (1995). Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. J. Cell Biol. 129, 397-410.
    • (1995) J. Cell Biol. , vol.129 , pp. 397-410
    • Turowski, P.1    Fernandez, A.2    Favre, B.3    Lamb, N.J.C.4    Hemmings, B.A.5
  • 63
    • 0031613906 scopus 로고    scopus 로고
    • Microinjection and immunological methods in the analysis of type 1 and 2A protein phosphatases from mammalian cells
    • Turowski, P., and Lamb, N.J.C (1998). Microinjection and immunological methods in the analysis of type 1 and 2A protein phosphatases from mammalian cells. Methods Mol. Biol. 93, 117-136.
    • (1998) Methods Mol. Biol. , vol.93 , pp. 117-136
    • Turowski, P.1    Lamb, N.J.C.2
  • 64
    • 0027256436 scopus 로고
    • Mutation of twins encoding a regulator of protein phosphatase 2A leads to pattern duplication in Drosophila imaginal disks
    • Uemura, T., Shiomi, K., Togashi, S., and Takeichi, M. (1993). Mutation of twins encoding a regulator of protein phosphatase 2A leads to pattern duplication in Drosophila imaginal disks. Genes & Dev. 7, 429-440.
    • (1993) Genes & Dev. , vol.7 , pp. 429-440
    • Uemura, T.1    Shiomi, K.2    Togashi, S.3    Takeichi, M.4
  • 65
    • 0031046069 scopus 로고    scopus 로고
    • Cdc55p, the B-type regulatory subunit of protein phosphatase 2A, has multiple functions in mitosis and is required for the kinetochore/spindle checkpoint in Saccharomyces cerevisiae
    • Wang, Y., and Burke, D.J. (1997). Cdc55p, the B-type regulatory subunit of protein phosphatase 2A, has multiple functions in mitosis and is required for the kinetochore/spindle checkpoint in Saccharomyces cerevisiae. Mol. Cell. Biol. 17, 620-626.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 620-626
    • Wang, Y.1    Burke, D.J.2
  • 66
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera, S., and 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
  • 68
    • 0030991668 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae homologs of the mammalian B and B′ subunits of protein phosphatase 2A direct the enzyme to distinct cellular functions
    • Zhao, Y., Boguslawski, G., Zitomer, R.S., and DePaoli-Roach, A.A. (1997). Saccharomyces cerevisiae homologs of the mammalian B and B′ subunits of protein phosphatase 2A direct the enzyme to distinct cellular functions. J. Biol. Chem. 272, 8256-8262.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8256-8262
    • Zhao, Y.1    Boguslawski, G.2    Zitomer, R.S.3    DePaoli-Roach, A.A.4
  • 69
    • 0028099583 scopus 로고
    • Diversity in the regulatory B-subunits of protein phosphatase 2A: Identification of a novel isoform highly expressed in brain
    • Zolnierowicz, S., Csortos, C., Bondor, J., Verin, A., Mumby, M.C., and DePaoli-Roach, A.A. (1994). Diversity in the regulatory B-subunits of protein phosphatase 2A: identification of a novel isoform highly expressed in brain. Biochemistry 33, 11858-11867.
    • (1994) Biochemistry , vol.33 , pp. 11858-11867
    • Zolnierowicz, S.1    Csortos, C.2    Bondor, J.3    Verin, A.4    Mumby, M.C.5    DePaoli-Roach, A.A.6


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