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Volumn 60, Issue 8, 2000, Pages 1225-1235

Type 2A protein phosphatase, the complex regulator of numerous signaling pathways

Author keywords

Cell cycle; Phosphatase inhibitors; Protein kinases; Protein phosphatase 2A; Protein phosphatases; Protein phosphorylation; Signal transduction; Transcription factors

Indexed keywords

ANTINEOPLASTIC AGENT; CERAMIDE; DIMER; FOSTRIECIN; HOLOENZYME; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOSERINE; PHOSPHOTHREONINE; PROTEIN INHIBITOR; PROTEIN KINASE; TRANSCRIPTION FACTOR;

EID: 0034668176     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(00)00424-X     Document Type: Article
Times cited : (180)

References (101)
  • 1
    • 0033598830 scopus 로고    scopus 로고
    • The protein kinases of Caenorhabditis elegans: A model for signal transduction in multicellular organisms
    • Plowman G.D., Sudarsanam S., Bingham J., Whyte D., Hunter T. The protein kinases of Caenorhabditis elegans A model for signal transduction in multicellular organisms . Proc Natl Acad Sci USA. 96:1999;13603-13610.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13603-13610
    • Plowman, G.D.1    Sudarsanam, S.2    Bingham, J.3    Whyte, D.4    Hunter, T.5
  • 2
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams M.D., et al. The genome sequence of Drosophila melanogaster. Science. 287:2000;2185-2195.
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1
  • 4
    • 0030790128 scopus 로고    scopus 로고
    • Novel protein serine/threonine phosphatases: Variety is the spice of life
    • Cohen P.T. Novel protein serine/threonine phosphatases Variety is the spice of life . Trends Biochem Sci. 22:1997;245-251.
    • (1997) Trends Biochem Sci , vol.22 , pp. 245-251
    • Cohen, P.T.1
  • 5
    • 0034651752 scopus 로고    scopus 로고
    • Protein phosphorylation and protein phosphatases. De Panne, Belgium, September 19-24, 1999
    • Zolnierowicz S., Bollen M. Protein phosphorylation and protein phosphatases. De Panne, Belgium, September 19-24, 1999. EMBO J. 19:2000;483-488.
    • (2000) EMBO J , vol.19 , pp. 483-488
    • Zolnierowicz, S.1    Bollen, M.2
  • 6
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem. 58:1989;453-508.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 7
    • 0027244764 scopus 로고
    • Protein serine/threonine phosphatases and cell transformation
    • Walter G., Mumby M. Protein serine/threonine phosphatases and cell transformation. Biochim Biophys Acta. 1155:1993;207-226.
    • (1993) Biochim Biophys Acta , vol.1155 , pp. 207-226
    • Walter, G.1    Mumby, M.2
  • 8
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases-new avenues for cell regulation
    • Shenolikar S. Protein serine/threonine phosphatases-new avenues for cell regulation. Annu Rev Cell Biol. 10:1994;55-86.
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 9
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera S., Hemmings B.A. Serine/threonine protein phosphatases. Biochem J. 311:1995;17-29.
    • (1995) Biochem J , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 10
    • 0030296869 scopus 로고    scopus 로고
    • Molecular mechanisms of the protein serine/threonine phosphatases
    • Barford D. Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci. 21:1996;407-412.
    • (1996) Trends Biochem Sci , vol.21 , pp. 407-412
    • Barford, D.1
  • 11
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades C by protein phosphatase 2A
    • Millward T.A., Zolnierowicz S., Hemmings B.A. Regulation of protein kinase cascades C by protein phosphatase 2A. Trends Biochem Sci. 24:1999;186-191.
    • (1999) Trends Biochem Sci , vol.24 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 12
    • 0032946279 scopus 로고    scopus 로고
    • Protein phosphatase 2A: Who shall regulate the regulator
    • Goldberg Y. Protein phosphatase 2A Who shall regulate the regulator . Biochem Pharmacol. 57:1999;321-328.
    • (1999) Biochem Pharmacol , vol.57 , pp. 321-328
    • Goldberg, Y.1
  • 14
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • Murata K., Wu J., Brautigan D.L. B cell receptor-associated protein alpha4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc Natl Acad Sci USA. 94:1997;10624-10629.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 16
    • 0031017969 scopus 로고    scopus 로고
    • Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: Abundant expression of both forms in cells
    • Kremmer E., Ohst K., Kiefer J., Brewis N., Walter G. Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit Abundant expression of both forms in cells . Mol Cell Biol. 17:1997;1692-1701.
    • (1997) Mol Cell Biol , vol.17 , pp. 1692-1701
    • Kremmer, E.1    Ohst, K.2    Kiefer, J.3    Brewis, N.4    Walter, G.5
  • 18
    • 0024557105 scopus 로고
    • Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes
    • Chen S.C., Kramer G., Hardesty B. Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes. J Biol Chem. 264:1989;7267-7275.
    • (1989) J Biol Chem , vol.264 , pp. 7267-7275
    • Chen, S.C.1    Kramer, G.2    Hardesty, B.3
  • 19
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D. The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell. 96:1999;99-110.
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 20
    • 0029808294 scopus 로고    scopus 로고
    • Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases
    • Di Como C.J., Arndt K.T. Nutrients, via the Tor proteins, stimulate the association of Tap42 with type 2A phosphatases. Genes Dev. 10:1996;1904-1916.
    • (1996) Genes Dev , vol.10 , pp. 1904-1916
    • Di Como, C.J.1    Arndt, K.T.2
  • 21
    • 0033577745 scopus 로고    scopus 로고
    • Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast
    • Jiang Y., Broach J.R. Tor proteins and protein phosphatase 2A reciprocally regulate Tap42 in controlling cell growth in yeast. EMBO J. 18:1999;2782-2792.
    • (1999) EMBO J , vol.18 , pp. 2782-2792
    • Jiang, Y.1    Broach, J.R.2
  • 22
    • 0033033091 scopus 로고    scopus 로고
    • Sakaguchi N, Hara K and Yonezawa K, Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases
    • Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S. Sakaguchi N, Hara K and Yonezawa K, Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases. FEBS LETT. 446:1999;108-112.
    • (1999) FEBS LETT , vol.446 , pp. 108-112
    • Nanahoshi, M.1    Tsujishita, Y.2    Tokunaga, C.3    Inui, S.4
  • 23
    • 0033213260 scopus 로고    scopus 로고
    • The Arabidopsis homolog of yeast TAP42 and mammalian alpha4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling
    • Harris D.M., Myrick T.L., Rundle S.J. The Arabidopsis homolog of yeast TAP42 and mammalian alpha4 binds to the catalytic subunit of protein phosphatase 2A and is induced by chilling. Plant Physiol. 121:1999;609-617.
    • (1999) Plant Physiol , vol.121 , pp. 609-617
    • Harris, D.M.1    Myrick, T.L.2    Rundle, S.J.3
  • 25
    • 0026661827 scopus 로고
    • Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus
    • Ruediger R., Roeckel D., Fait J., Bergqvist A., Magnusson G., Walter G. Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus. Mol Cell Biol. 12:1992;4872-4882.
    • (1992) Mol Cell Biol , vol.12 , pp. 4872-4882
    • Ruediger, R.1    Roeckel, D.2    Fait, J.3    Bergqvist, A.4    Magnusson, G.5    Walter, G.6
  • 26
    • 0028082299 scopus 로고
    • Molecular model of the A subunit of protein phosphatase 2A: Interaction with other subunits and tumor antigens
    • Ruediger R., Hentz M., Fait J., Mumby M., Walter G. Molecular model of the A subunit of protein phosphatase 2A Interaction with other subunits and tumor antigens . J Virol. 68:1994;123-129.
    • (1994) J Virol , vol.68 , pp. 123-129
    • Ruediger, R.1    Hentz, M.2    Fait, J.3    Mumby, M.4    Walter, G.5
  • 27
    • 0032703317 scopus 로고    scopus 로고
    • Chang D, Zaucha JA, Colbran RJ and Wadzinski BE, Cloning and characterization of B delta, a novel regulatory subunit of protein phosphatase 2A
    • Strack S. Chang D, Zaucha JA, Colbran RJ and Wadzinski BE, Cloning and characterization of B delta, a novel regulatory subunit of protein phosphatase 2A. FEBS Lett. 460:1999;462-466.
    • (1999) FEBS Lett , vol.460 , pp. 462-466
    • Strack, S.1
  • 28
    • 0033972224 scopus 로고    scopus 로고
    • PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells
    • Yan Z., Fedorov S.A., Mumby M.C., Williams R.S. PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells. Mol Cell Biol. 20:2000;1021-1029.
    • (2000) Mol Cell Biol , vol.20 , pp. 1021-1029
    • Yan, Z.1    Fedorov, S.A.2    Mumby, M.C.3    Williams, R.S.4
  • 29
    • 0028358381 scopus 로고
    • Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A
    • Cayla X., Van Hoof C., Bosch M., Waelkens E., Vandekerckhove J., Peeters B., Merlevede W., Goris J. Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A. J Biol Chem. 269:1994;15668-15675.
    • (1994) J Biol Chem , vol.269 , pp. 15668-15675
    • Cayla, X.1    Van Hoof, C.2    Bosch, M.3    Waelkens, E.4    Vandekerckhove, J.5    Peeters, B.6    Merlevede, W.7    Goris, J.8
  • 30
    • 0032555508 scopus 로고    scopus 로고
    • A yeast homologue of the human phosphotyrosyl phosphatase activator PTPA is implicated in protection against oxidative DNA damage induced by the model carcinogen 4-nitroquinoline 1-oxide
    • Ramotar D., Belanger E., Brodeur I., Masson J.Y., Drobetsky E.A. A yeast homologue of the human phosphotyrosyl phosphatase activator PTPA is implicated in protection against oxidative DNA damage induced by the model carcinogen 4-nitroquinoline 1-oxide. J Biol Chem. 273:1998;21489-21496.
    • (1998) J Biol Chem , vol.273 , pp. 21489-21496
    • Ramotar, D.1    Belanger, E.2    Brodeur, I.3    Masson, J.Y.4    Drobetsky, E.A.5
  • 31
    • 0027212627 scopus 로고
    • Phosphatase 2A associated with polyomavirus small-T or middle-T antigen is an okadaic acid-sensitive tyrosyl phosphatase
    • Cayla X., Ballmer-Hofer K., Merlevede W., Goris J. Phosphatase 2A associated with polyomavirus small-T or middle-T antigen is an okadaic acid-sensitive tyrosyl phosphatase. Eur J Biochem. 214:1993;281-286.
    • (1993) Eur J Biochem , vol.214 , pp. 281-286
    • Cayla, X.1    Ballmer-Hofer, K.2    Merlevede, W.3    Goris, J.4
  • 32
    • 0027277098 scopus 로고
    • On target with a new mechanism for the regulation of protein phosphorylation
    • Hubbard M.J., Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem Sci. 18:1993;172-177.
    • (1993) Trends Biochem Sci , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 33
    • 0034050449 scopus 로고    scopus 로고
    • WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A
    • Moreno C.S., Park S., Nelson K., Ashby D., Hubalek F., Lane W.S., Pallas D.C. WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A. J Biol Chem. 275:2000;5257-5263.
    • (2000) J Biol Chem , vol.275 , pp. 5257-5263
    • Moreno, C.S.1    Park, S.2    Nelson, K.3    Ashby, D.4    Hubalek, F.5    Lane, W.S.6    Pallas, D.C.7
  • 34
    • 0027337563 scopus 로고
    • Protein phosphatase 2A1 is the major enzyme in vertebrate cell extracts that dephosphorylates several physiological substrates for cyclin-dependent protein kinases
    • Ferrigno P., Langan T.A., Cohen P. Protein phosphatase 2A1 is the major enzyme in vertebrate cell extracts that dephosphorylates several physiological substrates for cyclin-dependent protein kinases. Mol Biol Cell. 4:1993;669-677.
    • (1993) Mol Biol Cell , vol.4 , pp. 669-677
    • Ferrigno, P.1    Langan, T.A.2    Cohen, P.3
  • 35
    • 0028276611 scopus 로고
    • Different oligomeric forms of protein phosphatase 2A activate and inhibit simian virus 40 DNA replication
    • Cegielska A., Shaffer S., Derua R., Goris J., Virshup D.M. Different oligomeric forms of protein phosphatase 2A activate and inhibit simian virus 40 DNA replication. Mol Cell Biol. 14:1994;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
  • 36
    • 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., Mumby M.C. A novel pool of protein phosphatase 2A is associated with microtubules and is regulated during the cell cycle. J Cell Biol. 128:1995;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
  • 37
    • 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., Virshup D.M. 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. 271:1996;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
  • 39
    • 0027184102 scopus 로고
    • Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase
    • Lee J., Stock J. Protein phosphatase 2A catalytic subunit is methyl-esterified at its carboxyl terminus by a novel methyltransferase. J Biol Chem. 268:1993;19192-19195.
    • (1993) J Biol Chem , vol.268 , pp. 19192-19195
    • Lee, J.1    Stock, J.2
  • 40
    • 0028154020 scopus 로고
    • Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain
    • Xie H., Clarke S. Protein phosphatase 2A is reversibly modified by methyl esterification at its C-terminal leucine residue in bovine brain. J Biol Chem. 269:1994;1981-1984.
    • (1994) J Biol Chem , vol.269 , pp. 1981-1984
    • Xie, H.1    Clarke, S.2
  • 41
    • 0028361380 scopus 로고
    • The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo
    • Favre B., Zolnierowicz S., Turowski P., Hemmings B.A. The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. J Biol Chem. 269:1994;16311-16317.
    • (1994) J Biol Chem , vol.269 , pp. 16311-16317
    • Favre, B.1    Zolnierowicz, S.2    Turowski, P.3    Hemmings, B.A.4
  • 42
    • 0033553570 scopus 로고    scopus 로고
    • A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
    • Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C. A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. J Biol Chem. 274:1999;14382-14391.
    • (1999) J Biol Chem , vol.274 , pp. 14382-14391
    • Ogris, E.1    Du, X.2    Nelson, K.C.3    Mak, E.K.4    Yu, X.X.5    Lane, W.S.6    Pallas, D.C.7
  • 43
    • 0033554835 scopus 로고    scopus 로고
    • Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue
    • De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E., Merlevede W., Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 38:1999;16539-16547.
    • (1999) Biochemistry , vol.38 , pp. 16539-16547
    • De Baere, I.1    Derua, R.2    Janssens, V.3    Van Hoof, C.4    Waelkens, E.5    Merlevede, W.6    Goris, J.7
  • 44
    • 0033560729 scopus 로고    scopus 로고
    • Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit
    • Bryant J.C., Westphal R.S., Wadzinski B.E. Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit. Biochem J. 339:1999;241-246.
    • (1999) Biochem J , vol.339 , pp. 241-246
    • Bryant, J.C.1    Westphal, R.S.2    Wadzinski, B.E.3
  • 45
    • 0028237871 scopus 로고
    • Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts
    • Chen J., Parsons S., Brautigan D.L. Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts. J Biol Chem. 269:1994;7957-7962.
    • (1994) J Biol Chem , vol.269 , pp. 7957-7962
    • Chen, J.1    Parsons, S.2    Brautigan, D.L.3
  • 46
    • 0027477103 scopus 로고
    • Autophospholylation-activated protein kinase phosphorylates and C inactivates protein phosphatase 2A
    • Guo H., Damuni Z. Autophospholylation-activated protein kinase phosphorylates and C inactivates protein phosphatase 2A. Proc Natl Acad Sci USA. 90:1993;2500-2504.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2500-2504
    • Guo, H.1    Damuni, Z.2
  • 47
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • Li M., Guo H., Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry. 34:1995;1988-1996.
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 48
    • 0029889342 scopus 로고    scopus 로고
    • The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A
    • Li M., Makkinje A., Damuni Z. The myeloid leukemia-associated protein SET is a potent inhibitor of protein phosphatase 2A. J Biol Chem. 271:1996;11059-11062.
    • (1996) J Biol Chem , vol.271 , pp. 11059-11062
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 50
    • 0028122397 scopus 로고
    • Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction
    • Wolff RA, Dobrowsky RT, Bielawska A, Obeid LM and Hannun YA, Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction. J Biol Chem269: 19605-19609, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 19605-19609
    • Wolff, R.A.1    Dobrowsky, R.T.2    Bielawska, A.3    Obeid, L.M.4    Hannun, Y.A.5
  • 52
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • Ruvolo P.P., Deng X., Ito T., Carr B.K., May W.S. Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A. J Biol Chem. 274:1999;20296-20300.
    • (1999) J Biol Chem , vol.274 , pp. 20296-20300
    • Ruvolo, P.P.1    Deng, X.2    Ito, T.3    Carr, B.K.4    May, W.S.5
  • 53
    • 0028131997 scopus 로고
    • Spatiotemporal distribution of protein kinase and phosphatase activities
    • Inagaki N., Ito M., Nakano T., Inagaki M. Spatiotemporal distribution of protein kinase and phosphatase activities. Trends Biochem Sci. 19:1994;448-452.
    • (1994) Trends Biochem Sci , vol.19 , pp. 448-452
    • Inagaki, N.1    Ito, M.2    Nakano, T.3    Inagaki, M.4
  • 54
    • 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., Lefkowitz R.J. The G-protein-coupled receptor phosphatase A protein phosphatase type 2A with a distinct subcellular distribution and substrate specificity . Proc Natl Acad Sci USA. 92:1995;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
  • 55
    • 0032978487 scopus 로고    scopus 로고
    • Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55
    • Turowski P., Myles T., Hemmings B.A., Fernandez A., Lamb N.J. Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol Biol Cell. 10:1999;1997-2015.
    • (1999) Mol Biol Cell , vol.10 , pp. 1997-2015
    • Turowski, P.1    Myles, T.2    Hemmings, B.A.3    Fernandez, A.4    Lamb, N.J.5
  • 56
    • 0034163509 scopus 로고    scopus 로고
    • Protein phosphatase 2A is associated in an inactive state with microtubules through 2A1-specific interaction with tubulin
    • Hiraga A., Tamura S. Protein phosphatase 2A is associated in an inactive state with microtubules through 2A1-specific interaction with tubulin. Biochem J. 346:2000;433-439.
    • (2000) Biochem J , vol.346 , pp. 433-439
    • Hiraga, A.1    Tamura, S.2
  • 57
    • 0032743059 scopus 로고    scopus 로고
    • An anchoring factor targets protein phosphatase 2A to brain microtubules
    • Price N.E., Wadzinski B., Mumby M.C. An anchoring factor targets protein phosphatase 2A to brain microtubules. Brain Res Mol Brain Res. 73:1999;68-77.
    • (1999) Brain Res Mol Brain Res , vol.73 , pp. 68-77
    • Price, N.E.1    Wadzinski, B.2    Mumby, M.C.3
  • 58
    • 0034008926 scopus 로고    scopus 로고
    • Transient translocation and activation of protein phosphatase 2A during mast cell secretion
    • Ludowyke R.I., Holst J., Mudge L.M., Sim A.T. Transient translocation and activation of protein phosphatase 2A during mast cell secretion. J Biol Chem. 275:2000;6144-6152.
    • (2000) J Biol Chem , vol.275 , pp. 6144-6152
    • Ludowyke, R.I.1    Holst, J.2    Mudge, L.M.3    Sim, A.T.4
  • 59
    • 0027272945 scopus 로고
    • Tumor promotion by inhibitors of protein phosphatases 1 and 2A: The okadaic acid class of compounds
    • Fujiki H., Suganuma M. Tumor promotion by inhibitors of protein phosphatases 1 and 2A The okadaic acid class of compounds . Adv Cancer Res. 61:1993;143-194.
    • (1993) Adv Cancer Res , vol.61 , pp. 143-194
    • Fujiki, H.1    Suganuma, M.2
  • 60
    • 0028089860 scopus 로고
    • Inhibitors of protein kinases and phosphatases
    • MacKintosh C., MacKintosh R.W. Inhibitors of protein kinases and phosphatases. Trends Biochem Sci. 19:1994;444-448.
    • (1994) Trends Biochem Sci , vol.19 , pp. 444-448
    • MacKintosh, C.1    MacKintosh, R.W.2
  • 61
    • 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., Hemmings B.A. 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. 272:1997;13856-13863.
    • (1997) J Biol Chem , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 62
    • 0032563347 scopus 로고    scopus 로고
    • Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters
    • Hastie C.J., Cohen P.T. Purification of protein phosphatase 4 catalytic subunit Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters . FEBS Lett. 431:1998;357-361.
    • (1998) FEBS Lett , vol.431 , pp. 357-361
    • Hastie, C.J.1    Cohen, P.T.2
  • 63
    • 0028133445 scopus 로고
    • A novel human protein 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., Cohen P.T. A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J. 13:1994;4278-4290.
    • (1994) EMBO J , vol.13 , 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
  • 65
  • 67
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376:1995;745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 69
    • 0033209692 scopus 로고    scopus 로고
    • The apoptosis-inducing activity of the two protein phosphatase inhibitors, tautomycin and thyrsiferyl 23-acetate, is not due to the inhibition of protein phosphatases PP1 and PP2A
    • Kikuchi K., Shima H., Mitsuhashi S., Suzuki M., Oikawa H. The apoptosis-inducing activity of the two protein phosphatase inhibitors, tautomycin and thyrsiferyl 23-acetate, is not due to the inhibition of protein phosphatases PP1 and PP2A. Int J Mol Med. 4:1999;395-401.
    • (1999) Int J Mol Med , vol.4 , pp. 395-401
    • Kikuchi, K.1    Shima, H.2    Mitsuhashi, S.3    Suzuki, M.4    Oikawa, H.5
  • 70
    • 0032729912 scopus 로고    scopus 로고
    • Cytostatin, an inhibitor of cell adhesion to extracellular matrix, selectively inhibits protein phosphatase 2A
    • Kawada M., Amemiya M., Ishizuka M., Takeuchi T. Cytostatin, an inhibitor of cell adhesion to extracellular matrix, selectively inhibits protein phosphatase 2A. Biochim Biophys Acta. 1452:1999;209-217.
    • (1999) Biochim Biophys Acta , vol.1452 , pp. 209-217
    • Kawada, M.1    Amemiya, M.2    Ishizuka, M.3    Takeuchi, T.4
  • 71
    • 0032832472 scopus 로고    scopus 로고
    • Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A
    • Meek S., Morrice N., MacKintosh C. Microcystin affinity purification of plant protein phosphatases PP1C, PP5 and a regulatory A-subunit of PP2A . FEBS Lett. 457:1999;494-498.
    • (1999) FEBS Lett , vol.457 , pp. 494-498
    • Meek, S.1    Morrice, N.2    MacKintosh, C.3
  • 72
    • 0026091769 scopus 로고
    • CDC55, a Saccharomyces 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., Pringle J.R. CDC55, a Saccharomyces cerevisiae gene involved in cellular morphogenesis Identification, characterization, and homology to the B subunit of mammalian type 2A protein phosphatase . Mol Cell Biol. 11:1991;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
  • 73
    • 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., Burke D.J. 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. 17:1997;620-626.
    • (1997) Mol Cell Biol , vol.17 , pp. 620-626
    • Wang, Y.1    Burke, D.J.2
  • 75
    • 0033552957 scopus 로고    scopus 로고
    • Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein
    • Voorhoeve P.M., Hijmans E.M., Bernards R. Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein. Oncogene. 18:1999;515-524.
    • (1999) Oncogene , vol.18 , pp. 515-524
    • Voorhoeve, P.M.1    Hijmans, E.M.2    Bernards, R.3
  • 77
    • 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., Hemmings B.A. The catalytic subunit of protein phosphatase 2A associates with the translation termination factor eRF1. EMBO J. 15:1996;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
  • 78
    • 0033255039 scopus 로고    scopus 로고
    • Eukaryotic translation termination factor 1 associates with protein phosphatase 2A and targets it to ribosomes
    • Lechward K., Zolnierowicz S., Hemmings B.A. Eukaryotic translation termination factor 1 associates with protein phosphatase 2A and targets it to ribosomes. Biochemistry (Moscow). 64:1999;1373-1381.
    • (1999) Biochemistry (Moscow) , vol.64 , pp. 1373-1381
    • Lechward, K.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 79
    • 0033527642 scopus 로고    scopus 로고
    • Distinct roles for PP1 and PP2A in phosphoiylation of the retinoblastoma protein. PP2A regulates the activities of G(1) cyclin-dependent kinases
    • Yan Y., Mumby M.C. Distinct roles for PP1 and PP2A in phosphoiylation of the retinoblastoma protein. PP2A regulates the activities of G(1) cyclin-dependent kinases. J Biol Chem. 274:1999;31917-31924.
    • (1999) J Biol Chem , vol.274 , pp. 31917-31924
    • Yan, Y.1    Mumby, M.C.2
  • 80
    • 0033021636 scopus 로고    scopus 로고
    • AKAPs: From structure to function
    • Colledge M., Scott J.D. AKAPs From structure to function . Trends Cell Biol. 9:1999;216-221.
    • (1999) Trends Cell Biol , vol.9 , pp. 216-221
    • Colledge, M.1    Scott, J.D.2
  • 81
    • 0033546152 scopus 로고    scopus 로고
    • Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus
    • Takahashi M., Shibata H., Shimakawa M., Miyamoto M., Mukai H., Ono Y. Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the Golgi apparatus. J Biol Chem. 274:1999;17267-17274.
    • (1999) J Biol Chem , vol.274 , pp. 17267-17274
    • Takahashi, M.1    Shibata, H.2    Shimakawa, M.3    Miyamoto, M.4    Mukai, H.5    Ono, Y.6
  • 82
    • 0033605639 scopus 로고    scopus 로고
    • Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A
    • Seeling J.M., Miller J.R., Gil R., Moon R.T., White R., Virshup D.M. Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science. 283:1999;2089-2091.
    • (1999) Science , vol.283 , pp. 2089-2091
    • Seeling, J.M.1    Miller, J.R.2    Gil, R.3    Moon, R.T.4    White, R.5    Virshup, D.M.6
  • 83
    • 0033524929 scopus 로고    scopus 로고
    • Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain
    • Hsu W., Zeng L., Costantini F. Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain. J Biol Chem. 274:1999;3439-3445.
    • (1999) J Biol Chem , vol.274 , pp. 3439-3445
    • Hsu, W.1    Zeng, L.2    Costantini, F.3
  • 84
    • 0034719170 scopus 로고    scopus 로고
    • GSK-3beta-dependent phosphorylation of adenomatous polyposis coli gene product can be modulated by beta-catenin and protein phosphatase 2A complexed with Axin
    • Ikeda S., Kishida M., Matsuura Y., Usui H., Kikuchi A. GSK-3beta-dependent phosphorylation of adenomatous polyposis coli gene product can be modulated by beta-catenin and protein phosphatase 2A complexed with Axin. Oncogene. 19:2000;537-545.
    • (2000) Oncogene , vol.19 , pp. 537-545
    • Ikeda, S.1    Kishida, M.2    Matsuura, Y.3    Usui, H.4    Kikuchi, A.5
  • 85
    • 0029348666 scopus 로고
    • Regulation of gene expression by serine/threonine protein phosphatases
    • Schonthal A.H. Regulation of gene expression by serine/threonine protein phosphatases. Semin Cancer Biol. 6:1995;239-248.
    • (1995) Semin Cancer Biol , vol.6 , pp. 239-248
    • Schonthal, A.H.1
  • 86
    • 0027221605 scopus 로고
    • Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation
    • Wadzinski B.E., Wheat W.H., Jaspers S., Peruski L.F. Jr, Lickteig R.L., Johnson G.L., Klemm D.J. Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation. Mol Cell Biol. 13:1993;2822-2834.
    • (1993) Mol Cell Biol , vol.13 , pp. 2822-2834
    • Wadzinski, B.E.1    Wheat, W.H.2    Jaspers, S.3    Peruski L.F., Jr.4    Lickteig, R.L.5    Johnson, G.L.6    Klemm, D.J.7
  • 87
    • 0028040416 scopus 로고
    • Simian virus 40 small tumor antigen inhibits dephosphorylation of protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation
    • Wheat W.H., Roesler W.J., Klemm D.J. Simian virus 40 small tumor antigen inhibits dephosphorylation of protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation. Mol Cell Biol. 14:1994;5881-5890.
    • (1994) Mol Cell Biol , vol.14 , pp. 5881-5890
    • Wheat, W.H.1    Roesler, W.J.2    Klemm, D.J.3
  • 88
    • 0028362018 scopus 로고
    • Expression of a peptide inhibitor of protein phosphatase 1 increases phosphorylation and activity of CREB in NIH 3T3 fibroblasts
    • Alberts A.S., Montminy M., Shenolikar S., Feramisco J.R. Expression of a peptide inhibitor of protein phosphatase 1 increases phosphorylation and activity of CREB in NIH 3T3 fibroblasts. Mol Cell Biol. 14:1994;4398-4407.
    • (1994) Mol Cell Biol , vol.14 , pp. 4398-4407
    • Alberts, A.S.1    Montminy, M.2    Shenolikar, S.3    Feramisco, J.R.4
  • 90
    • 0033565895 scopus 로고    scopus 로고
    • PP2A, an inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity
    • PP2A, an inhibitor of protein phosphatase 2A, induces c-Jun and AP-1 activity. Biochem J. 341:1999;293-298.
    • (1999) Biochem J , vol.341 , pp. 293-298
    • Al-Murrani, S.W.1    Woodgett, J.R.2    Damuni, Z.3
  • 91
    • 0034737501 scopus 로고    scopus 로고
    • Protein phosphatase 2A and phosphatidylinositol 3-kinase regulate the activity of Sp1-responsive promoters
    • Garcia A., Cereghini S., Sontag E. Protein phosphatase 2A and phosphatidylinositol 3-kinase regulate the activity of Sp1-responsive promoters. J Biol Chem. 275:2000;9385-9389.
    • (2000) J Biol Chem , vol.275 , pp. 9385-9389
    • Garcia, A.1    Cereghini, S.2    Sontag, E.3
  • 92
    • 0033538452 scopus 로고    scopus 로고
    • Regulation of angiotensin II-induced phosphorylation of STAT3 in vascular smooth muscle cells
    • Liang H., Venema V.J., Wang X., Ju H., Venema R.C., Marrero M.B. Regulation of angiotensin II-induced phosphorylation of STAT3 in vascular smooth muscle cells. J Biol Chem. 274:1999;19846-19851.
    • (1999) J Biol Chem , vol.274 , pp. 19846-19851
    • Liang, H.1    Venema, V.J.2    Wang, X.3    Ju, H.4    Venema, R.C.5    Marrero, M.B.6
  • 94
    • 0031031397 scopus 로고    scopus 로고
    • HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint
    • Kawabe T., Muslin A.J., Korsmeyer S.J. HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint. Nature. 385:1997;454-458.
    • (1997) Nature , vol.385 , pp. 454-458
    • Kawabe, T.1    Muslin, A.J.2    Korsmeyer, S.J.3
  • 95
    • 0032514680 scopus 로고    scopus 로고
    • Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Cα
    • Gotz J., Probst A., Ehler E., Hemmings B., Kues W. Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Cα Proc Natl Acad Sci USA. 95:1998;12370-12375.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12370-12375
    • Gotz, J.1    Probst, A.2    Ehler, E.3    Hemmings, B.4    Kues, W.5
  • 97
    • 0033621057 scopus 로고    scopus 로고
    • Induction of apoptosis by adenovirus E4orf4 protein is specific to transformed cells and requires an interaction with protein phosphatase 2A
    • Shtrichman R., Sharf R., Barr H., Dobner T., Kleinberger T. Induction of apoptosis by adenovirus E4orf4 protein is specific to transformed cells and requires an interaction with protein phosphatase 2A. Proc Natl Acad Sci USA. 96:1999;10080-10085.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10080-10085
    • Shtrichman, R.1    Sharf, R.2    Barr, H.3    Dobner, T.4    Kleinberger, T.5
  • 101
    • 0034708257 scopus 로고    scopus 로고
    • Low frequency of alterations of the alpha (PPP2R1A) and beta (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2A in human neoplasms
    • Calm G.A., di Iasio M.G., Caprini E., Vorechovsky I., Natali P.G., Sozzi G., Croce C.M., Barbanti-Brodano G., Russo G., Negrini M. Low frequency of alterations of the alpha (PPP2R1A) and beta (PPP2R1B) isoforms of the subunit A of the serine-threonine phosphatase 2A in human neoplasms. Oncogene. 24:2000;1191-1195.
    • (2000) Oncogene , vol.24 , pp. 1191-1195
    • Calm, G.A.1    Di Iasio, M.G.2    Caprini, E.3    Vorechovsky, I.4    Natali, P.G.5    Sozzi, G.6    Croce, C.M.7    Barbanti-Brodano, G.8    Russo, G.9    Negrini, M.10


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