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Volumn 403, Issue 1, 2007, Pages 149-156

Protein phosphorylation corrects the folding defect of the neuroblastoma (S120G) mutant of human nucleoside diphosphate kinase A/Nm23-H1

Author keywords

Folding intermediate; Histidine phosphorylation; Molten globule; Neuroblastoma; Nucleoside diphosphate (NDP) kinase (NM23)

Indexed keywords

BIOCHEMISTRY; CELLS; ESCHERICHIA COLI; MUTAGENESIS; PHOSPHORYLATION;

EID: 34147120195     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20061141     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 0036405268 scopus 로고    scopus 로고
    • Nucleoside-diphosphate kinase: Structural and kinetic analysis of reaction pathway and phosphohistidine intermediate
    • Janin, J. and Deville-Bonne, D. (2002) Nucleoside-diphosphate kinase: structural and kinetic analysis of reaction pathway and phosphohistidine intermediate. Methods Enzymol. 354, 118-134
    • (2002) Methods Enzymol , vol.354 , pp. 118-134
    • Janin, J.1    Deville-Bonne, D.2
  • 2
    • 0033795931 scopus 로고    scopus 로고
    • The catalytic mechanism of nucleoside diphosphate kinases
    • Lascu, I. and Gonin, P. (2000) The catalytic mechanism of nucleoside diphosphate kinases. J. Bioenerg. Biomembr. 32, 237-246
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 237-246
    • Lascu, I.1    Gonin, P.2
  • 3
    • 0025914104 scopus 로고
    • Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
    • Gilles, A. M., Presecan, E., Vonica, A. and Lascu, I. (1991) Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J. Biol. Chem. 266, 8784-8789
    • (1991) J. Biol. Chem , vol.266 , pp. 8784-8789
    • Gilles, A.M.1    Presecan, E.2    Vonica, A.3    Lascu, I.4
  • 4
    • 0029154302 scopus 로고
    • Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium
    • Morera, S., Chiadmi, M., LeBras, G., Lascu, I. and Janin, J. (1995) Mechanism of phosphate transfer by nucleoside diphosphate kinase: X-ray structures of the phosphohistidine intermediate of the enzymes from Drosophila and Dictyostelium. Biochemistry 34, 11062-11070
    • (1995) Biochemistry , vol.34 , pp. 11062-11070
    • Morera, S.1    Chiadmi, M.2    LeBras, G.3    Lascu, I.4    Janin, J.5
  • 5
    • 0033804989 scopus 로고    scopus 로고
    • Role of AWD/nucleoside diphosphate kinase in Drosophila development
    • Timmons, L. and Shearn, A. (2000) Role of AWD/nucleoside diphosphate kinase in Drosophila development. J. Bioenerg. Biomembr. 32, 293-300
    • (2000) J. Bioenerg. Biomembr , vol.32 , pp. 293-300
    • Timmons, L.1    Shearn, A.2
  • 6
    • 0037870275 scopus 로고    scopus 로고
    • Multiple biochemical activities of NM23/NDP kinase in gene regulation
    • Postel, E. H. (2003) Multiple biochemical activities of NM23/NDP kinase in gene regulation. J. Bioenerg. Biomembr. 35, 31-40
    • (2003) J. Bioenerg. Biomembr , vol.35 , pp. 31-40
    • Postel, E.H.1
  • 7
    • 2342445247 scopus 로고    scopus 로고
    • The metastasis suppressor NM23-H1 possesses 3′-5′ exonuclease activity
    • Ma, D., McCorkle, J. R. and Kaetzel, D. M. (2004) The metastasis suppressor NM23-H1 possesses 3′-5′ exonuclease activity. J. Biol. Chem. 279, 18073-18084
    • (2004) J. Biol. Chem , vol.279 , pp. 18073-18084
    • Ma, D.1    McCorkle, J.R.2    Kaetzel, D.M.3
  • 8
    • 0037423932 scopus 로고    scopus 로고
    • Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor
    • Fan, Z., Beresford, P. J., Oh, D. Y., Zhang, D. and Lieberman, J. (2003) Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell 112, 659-672
    • (2003) Cell , vol.112 , pp. 659-672
    • Fan, Z.1    Beresford, P.J.2    Oh, D.Y.3    Zhang, D.4    Lieberman, J.5
  • 11
    • 0025753514 scopus 로고
    • Reduced tumor incidence, metastatic potential, and cytokine responsiveness of nm23-transfected melanoma cells
    • Leone, A., Flatow, U., King, C. R., Sandeen, M. A., Margulies, I. M., Liotta, L. A. and Steeg, P. S. (1991) Reduced tumor incidence, metastatic potential, and cytokine responsiveness of nm23-transfected melanoma cells. Cell 65, 25-35
    • (1991) Cell , vol.65 , pp. 25-35
    • Leone, A.1    Flatow, U.2    King, C.R.3    Sandeen, M.A.4    Margulies, I.M.5    Liotta, L.A.6    Steeg, P.S.7
  • 14
    • 3543149047 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase A/nm23-H1 promotes metastasis of NB69-derived human neuroblastoma
    • Almgren, M. A., Henriksson, K. C., Fujimoto, J. and Chang, C. L. (2004) Nucleoside diphosphate kinase A/nm23-H1 promotes metastasis of NB69-derived human neuroblastoma. Mol. Cancer Res. 2, 387-394
    • (2004) Mol. Cancer Res , vol.2 , pp. 387-394
    • Almgren, M.A.1    Henriksson, K.C.2    Fujimoto, J.3    Chang, C.L.4
  • 15
    • 0038013876 scopus 로고    scopus 로고
    • Point mutations affecting the oligomeric structure of Nm23-H1 abrogates its inhibitory activity on colonization and invasion of prostate cancer cells
    • Kim, Y. I., Park, S., Jeoung, D. I. and Lee, H. (2003) Point mutations affecting the oligomeric structure of Nm23-H1 abrogates its inhibitory activity on colonization and invasion of prostate cancer cells. Biochem. Biophys. Res. Commun. 307, 281-289
    • (2003) Biochem. Biophys. Res. Commun , vol.307 , pp. 281-289
    • Kim, Y.I.1    Park, S.2    Jeoung, D.I.3    Lee, H.4
  • 17
    • 0033027431 scopus 로고    scopus 로고
    • Wild-type NM23-H1, but not its S120 mutants, suppresses desensitization of muscarinic potassium current
    • Otero, A. S., Doyle, M. B., Hartsough, M. T. and Steeg, P. S. (1999) Wild-type NM23-H1, but not its S120 mutants, suppresses desensitization of muscarinic potassium current. Biochim. Biophys. Acta 1449, 157-168
    • (1999) Biochim. Biophys. Acta , vol.1449 , pp. 157-168
    • Otero, A.S.1    Doyle, M.B.2    Hartsough, M.T.3    Steeg, P.S.4
  • 18
    • 0030905323 scopus 로고    scopus 로고
    • A point mutation of human nucleoside diphosphate kinase A found in aggressive neuroblastoma affects protein folding
    • Lascu, I., Schaertl, S., Wang, C., Sarger, C., Giartosio, A., Briand, G., Lacombe, M. L. and Konrad, M. (1997) A point mutation of human nucleoside diphosphate kinase A found in aggressive neuroblastoma affects protein folding. J. Biol. Chem. 272, 15599-15602
    • (1997) J. Biol. Chem , vol.272 , pp. 15599-15602
    • Lascu, I.1    Schaertl, S.2    Wang, C.3    Sarger, C.4    Giartosio, A.5    Briand, G.6    Lacombe, M.L.7    Konrad, M.8
  • 19
    • 0033575289 scopus 로고    scopus 로고
    • Human nucleoside diphosphate kinase B (Nm23-H2) from melanoma cells shows altered phosphoryl transfer activity due to the S122P mutation
    • Schaertl, S., Geeves, M. A. and Konrad, M. (1999) Human nucleoside diphosphate kinase B (Nm23-H2) from melanoma cells shows altered phosphoryl transfer activity due to the S122P mutation. J. Biol. Chem. 274, 20159-20164
    • (1999) J. Biol. Chem , vol.274 , pp. 20159-20164
    • Schaertl, S.1    Geeves, M.A.2    Konrad, M.3
  • 20
    • 0030046898 scopus 로고    scopus 로고
    • A nucleoside diphosphate kinase A (nm23-H1) serine 120 → glycine substitution in advanced stage neuroblastoma affects enzyme stability and alters protein-protein interaction
    • Chang, C. L., Strahler, J. R., Thoraval, D. H., Qian, M. G., Hinderer, R. and Hanash, S. M. (1996) A nucleoside diphosphate kinase A (nm23-H1) serine 120 → glycine substitution in advanced stage neuroblastoma affects enzyme stability and alters protein-protein interaction. Oncogene 12, 659-667
    • (1996) Oncogene , vol.12 , pp. 659-667
    • Chang, C.L.1    Strahler, J.R.2    Thoraval, D.H.3    Qian, M.G.4    Hinderer, R.5    Hanash, S.M.6
  • 21
    • 33845602708 scopus 로고    scopus 로고
    • Crystal structures of S120G mutant and wild type of human nucleoside diphosphate kinase A in complex with ADP
    • Giraud, M. F., Georgescauld, F., Lascu, I. and Dautant, A. (2006) Crystal structures of S120G mutant and wild type of human nucleoside diphosphate kinase A in complex with ADP. J. Bioenerg. Biomembr. 38, 261-264
    • (2006) J. Bioenerg. Biomembr , vol.38 , pp. 261-264
    • Giraud, M.F.1    Georgescauld, F.2    Lascu, I.3    Dautant, A.4
  • 23
    • 34147136610 scopus 로고    scopus 로고
    • Gonin, P. (2000) Nucleoside Diphosphate Kinases: Studies on the Catalytic Mechanism and Use as Hexamerization Domain in Protein Engineering. Ph.D. Thesis. University of Bordeaux-2, Bordeaux, France
    • Gonin, P. (2000) Nucleoside Diphosphate Kinases: Studies on the Catalytic Mechanism and Use as Hexamerization Domain in Protein Engineering. Ph.D. Thesis. University of Bordeaux-2, Bordeaux, France
  • 24
    • 0024103455 scopus 로고
    • Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila
    • Biggs, J., Tripoulas, N., Hersperger, E., Dearolf, C. and Shearn, A. (1988) Analysis of the lethal interaction between the prune and Killer of prune mutations of Drosophila. Genes Dev. 2, 1333-1343
    • (1988) Genes Dev , vol.2 , pp. 1333-1343
    • Biggs, J.1    Tripoulas, N.2    Hersperger, E.3    Dearolf, C.4    Shearn, A.5
  • 25
    • 0026708128 scopus 로고
    • A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation Killer of prune) affects stability but not catalytic efficiency of the enzyme
    • Lascu, I., Chaffotte, A., Limbourg-Bouchon, B. and Véron, M. (1992) A Pro/Ser substitution in nucleoside diphosphate kinase of Drosophila melanogaster (mutation Killer of prune) affects stability but not catalytic efficiency of the enzyme. J. Biol. Chem. 267, 12775-12781
    • (1992) J. Biol. Chem , vol.267 , pp. 12775-12781
    • Lascu, I.1    Chaffotte, A.2    Limbourg-Bouchon, B.3    Véron, M.4
  • 26
    • 0021094215 scopus 로고
    • Pig heart nucleosidediphosphate kinase: Phosphorylation and interaction with Cibacron blue 3GA
    • Lascu, I., Pop, R. D., Porumb, H., Presecan, E. and Proinov, I. (1983) Pig heart nucleosidediphosphate kinase: phosphorylation and interaction with Cibacron blue 3GA. Eur. J. Biochem. 135, 497-503
    • (1983) Eur. J. Biochem , vol.135 , pp. 497-503
    • Lascu, I.1    Pop, R.D.2    Porumb, H.3    Presecan, E.4    Proinov, I.5
  • 27
    • 0026347515 scopus 로고
    • Identification of phosphohistidine in proteins and purification of protein-histidine kinases
    • Wei, Y. F. and Matthews, H. R. (1991) Identification of phosphohistidine in proteins and purification of protein-histidine kinases. Methods Enzymol. 200, 388-414
    • (1991) Methods Enzymol , vol.200 , pp. 388-414
    • Wei, Y.F.1    Matthews, H.R.2
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem. 182, 319-326
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 29
    • 0027198008 scopus 로고
    • Equilibrium dissociation and unfolding of nucleoside diphosphate kinase from Dictyostelium discoideum
    • Lascu, I., Deville-Bonne, D., Glaser, P. and Veron, M. (1993) Equilibrium dissociation and unfolding of nucleoside diphosphate kinase from Dictyostelium discoideum. J. Biol. Chem. 268, 20268-20275
    • (1993) J. Biol. Chem , vol.268 , pp. 20268-20275
    • Lascu, I.1    Deville-Bonne, D.2    Glaser, P.3    Veron, M.4
  • 32
    • 0028286474 scopus 로고
    • Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi, L., Palleros, D. R. and Fink, A. L. (1994) Protein conformational changes induced by 1,1′-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Biochemistry 33, 7536-7546
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 33
  • 34
    • 33845657454 scopus 로고    scopus 로고
    • Nm23-H1/NDP kinase folding intermediates and cancer: A hypothesis
    • Lascu, I. (2006) Nm23-H1/NDP kinase folding intermediates and cancer: a hypothesis. J. Bioenerg. Biomembr. 38, 265-268
    • (2006) J. Bioenerg. Biomembr , vol.38 , pp. 265-268
    • Lascu, I.1
  • 35
    • 0348111209 scopus 로고    scopus 로고
    • Quaternary structure of Dictyostelium discoideum nucleoside diphosphate kinase counteracts the tendency of monomers to form a molten globule
    • Cervoni, L., Egistelli, L., Mocan, I., Giartosio, A. and Lascu, I. 2003 Quaternary structure of Dictyostelium discoideum nucleoside diphosphate kinase counteracts the tendency of monomers to form a molten globule. Biochemistry 42, 14599-14605
    • (2003) Biochemistry , vol.42 , pp. 14599-14605
    • Cervoni, L.1    Egistelli, L.2    Mocan, I.3    Giartosio, A.4    Lascu, I.5
  • 36
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis, J. R. (2001) Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26, 597-604
    • (2001) Trends Biochem. Sci , vol.26 , pp. 597-604
    • Ellis, J.R.1
  • 37
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution: A 60-year-old hypothesis revisited
    • James, L. C. and Tawfik, D. S. (2003) Conformational diversity and protein evolution: a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28, 361-368
    • (2003) Trends Biochem. Sci , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 39
    • 0029786618 scopus 로고    scopus 로고
    • Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    • Uversky, V. N., Kutyshenko, V. P., Protasova, N. Yu., Rogov, V. V., Vassilenko, K. S. and Gudkov, A. T. (1996) Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands. Protein Sci. 5, 1844-1851
    • (1996) Protein Sci , vol.5 , pp. 1844-1851
    • Uversky, V.N.1    Kutyshenko, V.P.2    Protasova, N.Y.3    Rogov, V.V.4    Vassilenko, K.S.5    Gudkov, A.T.6
  • 40
    • 14844322304 scopus 로고    scopus 로고
    • Last in, first out: The role of cofactor binding in flavodoxin folding
    • Bollen, Y. J., Nabuurs, S. M., van Berkel, W. J. and van Mierlo, C. P.(2005) Last in, first out: the role of cofactor binding in flavodoxin folding. J. Biol. Chem. 280, 7836-7844
    • (2005) J. Biol. Chem , vol.280 , pp. 7836-7844
    • Bollen, Y.J.1    Nabuurs, S.M.2    van Berkel, W.J.3    van Mierlo, C.P.4
  • 41
    • 0035814892 scopus 로고    scopus 로고
    • Cofactor-induced refolding: Refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II)
    • Andersson, D., Hammarstrom, P. and Carlsson, U. (2001) Cofactor-induced refolding: refolding of molten globule carbonic anhydrase induced by Zn(II) and Co(II). Biochemistry 40, 2653-2661
    • (2001) Biochemistry , vol.40 , pp. 2653-2661
    • Andersson, D.1    Hammarstrom, P.2    Carlsson, U.3
  • 42
    • 33645506272 scopus 로고    scopus 로고
    • Cofactor effects on the protein folding reaction: Acceleration of α-lactalbumin refolding by metal ions
    • Bushmarina, N. A., Blanchet, C. E., Vernier, G. and Forge, V. (2006) Cofactor effects on the protein folding reaction: acceleration of α-lactalbumin refolding by metal ions. Protein Sci. 15, 659-671
    • (2006) Protein Sci , vol.15 , pp. 659-671
    • Bushmarina, N.A.1    Blanchet, C.E.2    Vernier, G.3    Forge, V.4


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