메뉴 건너뛰기




Volumn 126, Issue 3, 1999, Pages 632-638

Interconversion of Mn2+-dependent and -independent protein phosphatase 2A from human erythrocytes: Role of Zn2+ and Fe2+ in protein phosphatase 2A

Author keywords

Fluoride; Protein phosphatase 2A; Vanadate; Zinc and iron metalloenzyme; Zinc metallothionein

Indexed keywords

ERYTHROCYTE ENZYME; FERROUS CHLORIDE; FERROUS ION; FLUORIDE SODIUM; MANGANESE; PHOSPHOPROTEIN PHOSPHATASE 2A; ZINC CHLORIDE; ZINC ION;

EID: 0032826338     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022495     Document Type: Article
Times cited : (7)

References (34)
  • 1
    • 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
  • 2
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby, M.C. and Walter, G. (1993) Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth. Physiol. Rev. 73, 673-699
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 3
    • 0023871140 scopus 로고
    • Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol
    • Usui, H., Imazu, M., Maeta, K., Tsukamoto, H., Azuma, K., and Takeda, M. (1988) Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol. J. Biol. Chem. 263, 3752-3761
    • (1988) J. Biol. Chem. , vol.263 , pp. 3752-3761
    • Usui, H.1    Imazu, M.2    Maeta, K.3    Tsukamoto, H.4    Azuma, K.5    Takeda, M.6
  • 4
    • 0027279893 scopus 로고
    • Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A: Evidence for different size forms produced by alternative splicing
    • Hendrix, P., Mayer-Jaekel, R.E., Cron, P., Goris, J., Hofsteenge, J., Merlevede, W., and Hemmings, B.A. (1993) Structure and expression of a 72-kDa regulatory subunit of protein phosphatase 2A: Evidence for different size forms produced by alternative splicing. J. Biol. Chem. 268, 15267-15276
    • (1993) J. Biol. Chem. , vol.268 , pp. 15267-15276
    • Hendrix, P.1    Mayer-Jaekel, R.E.2    Cron, P.3    Goris, J.4    Hofsteenge, J.5    Merlevede, W.6    Hemmings, B.A.7
  • 5
    • 0030977373 scopus 로고    scopus 로고
    • Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A
    • Tanabe, O., Gomez, G.A., Nishito, Y., Usui, H., and Takeda, M. (1997) Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory subunit (B″ or δ) of human protein phosphatase 2A. FEBS Lett. 408, 52-56
    • (1997) FEBS Lett. , vol.408 , pp. 52-56
    • Tanabe, O.1    Gomez, G.A.2    Nishito, Y.3    Usui, H.4    Takeda, M.5
  • 6
    • 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
  • 8
    • 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
  • 10
    • 0031032914 scopus 로고    scopus 로고
    • Identification of autophosphorylation sites in c-Yes purified from rat liver plasma membranes
    • Ariki, M., Tanabe, O., Usui, H., Hayashi, H., Inoue, R., Nishito, Y., Kagamiyama, H., and Takeda, M. (1997) Identification of autophosphorylation sites in c-Yes purified from rat liver plasma membranes. J. Biochem. 121, 104-111
    • (1997) J. Biochem. , vol.121 , pp. 104-111
    • Ariki, M.1    Tanabe, O.2    Usui, H.3    Hayashi, H.4    Inoue, R.5    Nishito, Y.6    Kagamiyama, H.7    Takeda, M.8
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation 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
  • 13
    • 0021099075 scopus 로고
    • Separation of multiple phosphotyrosyl- and phosphoseryl-protein phosphatases from chicken brain
    • Foulkes, J.G., Erikson, E., and Erikson, R.L. (1983) Separation of multiple phosphotyrosyl- and phosphoseryl-protein phosphatases from chicken brain. J. Biol. Chem. 258, 431-438
    • (1983) J. Biol. Chem. , vol.258 , pp. 431-438
    • Foulkes, J.G.1    Erikson, E.2    Erikson, R.L.3
  • 14
    • 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., and Goris, J. (1994) Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A. J. Biol. Chem. 269, 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
  • 15
    • 0001941317 scopus 로고
    • The physiological function of metallothionein
    • Brady, F.O. (1982) The physiological function of metallothionein. Trends Biochem. Sci. 7, 143-145
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 143-145
    • Brady, F.O.1
  • 16
    • 0031823639 scopus 로고    scopus 로고
    • 2+/ascorbate system
    • 2+/ascorbate system. J. Biochem. 124, 225-230
    • (1998) J. Biochem. , vol.124 , pp. 225-230
    • Yu, J.-S.1
  • 17
    • 0028838971 scopus 로고
    • Protein kinases andphosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. (1995) Protein kinases andphosphatases: The yin and yang of protein phosphorylation and signaling. Cell 80, 225-236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 19
    • 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., and Kuriyan, J. (1995) Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 376, 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
  • 20
    • 0029583122 scopus 로고
    • Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate
    • Egloff, M.-P., Cohen, P.T.W., Reinemer, P., and Barford, D. (1995) Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254, 942-959
    • (1995) J. Mol. Biol. , vol.254 , pp. 942-959
    • Egloff, M.-P.1    Cohen, P.T.W.2    Reinemer, P.3    Barford, D.4
  • 23
    • 0021367556 scopus 로고
    • Phosphorylase phosphatase: Interconversion of active and inactive forms
    • Villa-Moruzzi, E., Ballou, L.M., and Fischer, E.H. (1984) Phosphorylase phosphatase: Interconversion of active and inactive forms. J. Biol. Chem. 259, 5857-5863
    • (1984) J. Biol. Chem. , vol.259 , pp. 5857-5863
    • Villa-Moruzzi, E.1    Ballou, L.M.2    Fischer, E.H.3
  • 24
    • 0028061142 scopus 로고
    • A latent form of protein phosphatase 1α associated with bovine heart myofibrils
    • Chu, Y., Wilson, S.E., and Schlender, K.K. (1994) A latent form of protein phosphatase 1α associated with bovine heart myofibrils. Biochim. Biophys. Acta 1208, 45-54
    • (1994) Biochim. Biophys. Acta , vol.1208 , pp. 45-54
    • Chu, Y.1    Wilson, S.E.2    Schlender, K.K.3
  • 25
    • 0026567879 scopus 로고
    • Expression of the catalytic subunit of phosphorylase phosphatase (protein phosphatase-1) in Escherichia coli
    • Zhang, Z., Bai, G., Deans-Zirattu, S., Browner, M.F., and Lee, E.Y.C. (1992) Expression of the catalytic subunit of phosphorylase phosphatase (protein phosphatase-1) in Escherichia coli. J. Biol. Chem. 267, 1484-1490
    • (1992) J. Biol. Chem. , vol.267 , pp. 1484-1490
    • Zhang, Z.1    Bai, G.2    Deans-Zirattu, S.3    Browner, M.F.4    Lee, E.Y.C.5
  • 26
    • 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., and 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
  • 27
    • 0030070936 scopus 로고    scopus 로고
    • Activation of protein phosphatase 1: Formation of a metalloenzyme
    • Chu, Y., Lee, E.Y.C., and Schlender, K.K. (1996) Activation of protein phosphatase 1: Formation of a metalloenzyme. J. Biol. Chem. 271, 2574-2577
    • (1996) J. Biol. Chem. , vol.271 , pp. 2574-2577
    • Chu, Y.1    Lee, E.Y.C.2    Schlender, K.K.3
  • 28
    • 0029759409 scopus 로고    scopus 로고
    • Superoxide dismutase protects calcineurin from inactivation
    • Wang, X., Culotta, V.C., and Klee, C.B. (1996) Superoxide dismutase protects calcineurin from inactivation. Nature 383, 434-437
    • (1996) Nature , vol.383 , pp. 434-437
    • Wang, X.1    Culotta, V.C.2    Klee, C.B.3
  • 29
    • 0032499537 scopus 로고    scopus 로고
    • 2+ forms of bovine spleen purple acid phosphatase
    • 2+ forms of bovine spleen purple acid phosphatase. Biochemistry 37, 8490-8497
    • (1998) Biochemistry , vol.37 , pp. 8490-8497
    • Merkx, M.1    Averill, B.A.2
  • 30
    • 0030006123 scopus 로고    scopus 로고
    • Reversible zinc exchange between metallothionein and the estrogen receptor zinc finger
    • Cano-Gauci, D.F. and Sarkar, B. (1996) Reversible zinc exchange between metallothionein and the estrogen receptor zinc finger. FEBS Lett. 386, 1-4
    • (1996) FEBS Lett. , vol.386 , pp. 1-4
    • Cano-Gauci, D.F.1    Sarkar, B.2
  • 32
    • 0344945971 scopus 로고
    • An acid phosphatase in the plasma membranes of human astrocytoma showing marked specificity toward phosphotyrosine protein
    • Leis, J.F. and Kaplan, N.O. (1982) An acid phosphatase in the plasma membranes of human astrocytoma showing marked specificity toward phosphotyrosine protein. Proc. Natl. Acad. Sci. USA 79, 6507-6511
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6507-6511
    • Leis, J.F.1    Kaplan, N.O.2
  • 33
  • 34
    • 0030297891 scopus 로고    scopus 로고
    • Form and function in protein dephosphorylation
    • Denu, J.M., Stuckey, J.A., Saper, M.A., and Dixon, J.E. (1996) Form and function in protein dephosphorylation. Cell 87, 361-364
    • (1996) Cell , vol.87 , pp. 361-364
    • Denu, J.M.1    Stuckey, J.A.2    Saper, M.A.3    Dixon, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.