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Volumn 35, Issue 6, 2003, Pages 556-564

Protein kinase CK2 phosphorylates and interacts with deoxyhypusine synthase in HeLa cells

Author keywords

Eukaryotic initiation factor 5A; Phosphoamino acids; Phosphorylation; Post translational modification; Protein kinases; Protein processing

Indexed keywords

CASEIN KINASE II; DEOXYHYPUSINE SYNTHASE; GLUTAMIC ACID; HEPARIN; PHOSPHOAMINO ACID; POLYLYSINE; SERINE; SYNTHETASE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 1642542002     PISSN: 12263613     EISSN: 20926413     Source Type: Journal    
DOI: 10.1038/emm.2003.73     Document Type: Article
Times cited : (4)

References (47)
  • 2
    • 0035316766 scopus 로고    scopus 로고
    • Toward the phosphoproteome
    • Ahn NG, Resing KA. Toward the phosphoproteome. Nat Biotechnol 2001;19:317-8
    • (2001) Nat Biotechnol , vol.19 , pp. 317-318
    • Ahn, N.G.1    Resing, K.A.2
  • 3
    • 0028909420 scopus 로고
    • Protein kinases. 4. Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation
    • Allende JE, Allende CC. Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J 1995;9:313-23
    • (1995) FASEB J , vol.9 , pp. 313-323
    • Allende, J.E.1    Allende, C.C.2
  • 4
    • 0026778636 scopus 로고
    • Purification and characterization of casein kinase II (CKII) from delta ckal delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo
    • Bidwai AP, Hanna DE, Glover CV. Purification and characterization of casein kinase II (CKII) from delta ckal delta cka2 Saccharomyces cerevisiae rescued by Drosophila CKII subunits. The free catalytic subunit of casein kinase II is not toxic in vivo. J Biol Chem 1992;267:18790-6
    • (1992) J Biol Chem , vol.267 , pp. 18790-18796
    • Bidwai, A.P.1    Hanna, D.E.2    Glover, C.V.3
  • 5
    • 0027970532 scopus 로고
    • The role of hypusine depletion in cytostasis induced by S-adenosyl-L-methionine decarboxylase inhibition: New evidence provided by 1-methylspermidine and 1,12-dimethylspermine
    • Byers TL, Lakanen JR, Coward JK, Pegg AE. The role of hypusine depletion in cytostasis induced by S-adenosyl-L-methionine decarboxylase inhibition: new evidence provided by 1-methylspermidine and 1,12-dimethylspermine. Biochem J 1994;303:363-8
    • (1994) Biochem J , vol.303 , pp. 363-368
    • Byers, T.L.1    Lakanen, J.R.2    Coward, J.K.3    Pegg, A.E.4
  • 6
    • 0030817535 scopus 로고    scopus 로고
    • Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A
    • Chen KY, Liu AY. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol Signals 1997;6:105-9
    • (1997) Biol Signals , vol.6 , pp. 105-109
    • Chen, K.Y.1    Liu, A.Y.2
  • 7
    • 0025935237 scopus 로고
    • Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis
    • Duclos B, Marcandier S, Cozzone AJ. Chemical properties and separation of phosphoamino acids by thin-layer chromatography and/or electrophoresis. Methods Enzymol 1991;201:10-21
    • (1991) Methods Enzymol , vol.201 , pp. 10-21
    • Duclos, B.1    Marcandier, S.2    Cozzone, A.J.3
  • 8
    • 0025796976 scopus 로고
    • Isolation and characterization of recombinant human casein kinase II subunits alpha and beta from bacteria
    • Grankowski N, Boldyreff B, Issinger OG. Isolation and characterization of recombinant human casein kinase II subunits alpha and beta from bacteria. Eur J Biochem 1991;198:25-30
    • (1991) Eur J Biochem , vol.198 , pp. 25-30
    • Grankowski, N.1    Boldyreff, B.2    Issinger, O.G.3
  • 10
    • 0020437026 scopus 로고
    • Casein kinases-multipotential protein kinases
    • Hathaway GM, Traugh JA. Casein kinases-multipotential protein kinases. Curr Top Cell Regul 1982;21:101-27
    • (1982) Curr Top Cell Regul , vol.21 , pp. 101-127
    • Hathaway, G.M.1    Traugh, J.A.2
  • 11
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell 2000;100:113-27
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 12
    • 0000134797 scopus 로고
    • Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins
    • Joe YA, Wolff EC, Park MH. Cloning and expression of human deoxyhypusine synthase cDNA. Structure-function studies with the recombinant enzyme and mutant proteins. J Biol Chem 1995;270:22386-92
    • (1995) J Biol Chem , vol.270 , pp. 22386-22392
    • Joe, Y.A.1    Wolff, E.C.2    Park, M.H.3
  • 13
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins
    • Kamps MP, Sefton BM. Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Anal Biochem 1989;176:22-7
    • (1989) Anal Biochem , vol.176 , pp. 22-27
    • Kamps, M.P.1    Sefton, B.M.2
  • 14
    • 0027236378 scopus 로고
    • Translation initiation factor eIF-5A, the hypusine-containing protein, is phosphorylated on serine in Saccharomyces cerevisiae
    • Kang HA, Schwelberger HG, Hershey JW. Translation initiation factor eIF-5A, the hypusine-containing protein, is phosphorylated on serine in Saccharomyces cerevisiae. J Biol Chem 1993;268:14750-6
    • (1993) J Biol Chem , vol.268 , pp. 14750-14756
    • Kang, H.A.1    Schwelberger, H.G.2    Hershey, J.W.3
  • 15
    • 0029162976 scopus 로고
    • Identification of YHR068w in Saccharomyces cerevisiae chromosome VIII as a gene for deoxyhypusine synthase. Expression and characterization of the enzyme
    • Kang KR, Wolff EC, Park MH, Folk JE, Chung SI. Identification of YHR068w in Saccharomyces cerevisiae chromosome VIII as a gene for deoxyhypusine synthase. Expression and characterization of the enzyme. J Biol Chem 1995;270:18408-12
    • (1995) J Biol Chem , vol.270 , pp. 18408-18412
    • Kang, K.R.1    Wolff, E.C.2    Park, M.H.3    Folk, J.E.4    Chung, S.I.5
  • 16
    • 0033621369 scopus 로고    scopus 로고
    • Characterization of yeast deoxyhypusine synthase: PKC-dependent phosphorylation in vitro and functional domain identification
    • Kang KR, Chung SI. Characterization of yeast deoxyhypusine synthase: PKC-dependent phosphorylation in vitro and functional domain identification. Exp Mol Med 1999;31:210-6
    • (1999) Exp Mol Med , vol.31 , pp. 210-216
    • Kang, K.R.1    Chung, S.I.2
  • 17
    • 0037207239 scopus 로고    scopus 로고
    • Deoxyhypusine synthase is phosphorylated by protein kinase C in vivo as well as in vitro
    • Kang KR, Kim JS, Chung SI, Park MH, Kim YW, Lim D, Lee SY. Deoxyhypusine synthase is phosphorylated by protein kinase C in vivo as well as in vitro. Exp Mol Med 2002;34:489-95
    • (2002) Exp Mol Med , vol.34 , pp. 489-495
    • Kang, K.R.1    Kim, J.S.2    Chung, S.I.3    Park, M.H.4    Kim, Y.W.5    Lim, D.6    Lee, S.Y.7
  • 18
    • 0027997895 scopus 로고
    • The growth of research on protein phosphorylation
    • Krebs EG. The growth of research on protein phosphorylation. Trends Biochem Sci 1994;19:439
    • (1994) Trends Biochem Sci , vol.19 , pp. 439
    • Krebs, E.G.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander ES, Linton LM, Birren B, et al., International Human Genome Sequencing Consortium. Initial sequencing and analysis of the human genome. Nature 2001;409:860-921
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1    Linton, L.M.2    Birren, B.3
  • 21
    • 0029133121 scopus 로고
    • Diamine and triamine analogs and derivatives as inhibitors of deoxyhypusine synthase: Synthesis and biological activity
    • Lee YB, Park MH, Folk JE. Diamine and triamine analogs and derivatives as inhibitors of deoxyhypusine synthase: synthesis and biological activity. J Med Chem 1995;38:3053-61
    • (1995) J Med Chem , vol.38 , pp. 3053-3061
    • Lee, Y.B.1    Park, M.H.2    Folk, J.E.3
  • 22
    • 0026508869 scopus 로고
    • Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme
    • Meggio F, Boldyreff B, Marin O, Pinna LA, Issinger OG. Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur J Biochem 1992;204:293-7
    • (1992) Eur J Biochem , vol.204 , pp. 293-297
    • Meggio, F.1    Boldyreff, B.2    Marin, O.3    Pinna, L.A.4    Issinger, O.G.5
  • 23
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • Meggio F, Marin O, Pinna LA. Substrate specificity of protein kinase CK2. Cell Mol Biol Res 1994a;40:401-9
    • (1994) Cell Mol Biol Res , vol.40 , pp. 401-409
    • Meggio, F.1    Marin, O.2    Pinna, L.A.3
  • 24
    • 0028292988 scopus 로고
    • Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate
    • Meggio F, Boldyreff B, Issinger OG, Pinna LA. Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 region of the beta-subunit. A study with calmodulin as phosphorylatable substrate. Biochemistry 1994b;33:4336-42
    • (1994) Biochemistry , vol.33 , pp. 4336-4342
    • Meggio, F.1    Boldyreff, B.2    Issinger, O.G.3    Pinna, L.A.4
  • 25
    • 0033593052 scopus 로고    scopus 로고
    • Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase
    • Ober D, Hartmann T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc Natl Acad Sci USA 1999a;96:14777-82
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14777-14782
    • Ober, D.1    Hartmann, T.2
  • 26
    • 0033527751 scopus 로고    scopus 로고
    • Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity
    • Ober D, Hartmann T. Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity. J Biol Chem 1999b;274:32040-7
    • (1999) J Biol Chem , vol.274 , pp. 32040-32047
    • Ober, D.1    Hartmann, T.2
  • 27
    • 0034534251 scopus 로고    scopus 로고
    • Phylogenetic origin of a secondary pathway: The case of pyrrolizidine alkaloids
    • Ober D, Hartmann T. Phylogenetic origin of a secondary pathway: the case of pyrrolizidine alkaloids. Plant Mol Biol 2000;44:445-50
    • (2000) Plant Mol Biol , vol.44 , pp. 445-450
    • Ober, D.1    Hartmann, T.2
  • 28
    • 0038305967 scopus 로고    scopus 로고
    • Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein
    • Ober D, Harms R, Witte L, Hartmann T. Molecular evolution by change of function. Alkaloid-specific homospermidine synthase retained all properties of deoxyhypusine synthase except binding the eIF5A precursor protein. J Biol Chem 2003;278:12805-12
    • (2003) J Biol Chem , vol.278 , pp. 12805-12812
    • Ober, D.1    Harms, R.2    Witte, L.3    Hartmann, T.4
  • 29
    • 0041355635 scopus 로고    scopus 로고
    • Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase
    • Park JH, Wolff EC, Folk JE, Park MH. Reversal of the deoxyhypusine synthesis reaction. Generation of spermidine or homospermidine from deoxyhypusine by deoxyhypusine synthase. J Biol Chem 2003;278:32683-91
    • (2003) J Biol Chem , vol.278 , pp. 32683-32691
    • Park, J.H.1    Wolff, E.C.2    Folk, J.E.3    Park, M.H.4
  • 30
    • 0023723494 scopus 로고
    • Cell-free synthesis of deoxyhypusine. Separation of protein substrate and enzyme and identification of 1,3-diaminopropane as a product of spermidine cleavage
    • Park MH, Wolff EC. Cell-free synthesis of deoxyhypusine. Separation of protein substrate and enzyme and identification of 1,3-diaminopropane as a product of spermidine cleavage. J Biol Chem 1988;263:15264-9
    • (1988) J Biol Chem , vol.263 , pp. 15264-15269
    • Park, M.H.1    Wolff, E.C.2
  • 32
    • 0027197906 scopus 로고
    • Hypusine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation
    • Park MH, Wolff EC, Folk JE. Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation. Biofactors 1993a;4:95-104
    • (1993) Biofactors , vol.4 , pp. 95-104
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 33
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • Park MH, Wolff EC, Folk JE. Is hypusine essential for eukaryotic cell proliferation? Trends Biochem Sci 1993b;18:475-9
    • (1993) Trends Biochem Sci , vol.18 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 34
    • 0027944561 scopus 로고
    • Antiproliferative effects of inhibitors of deoxyhypusine synthase. Inhibition of growth of Chinese hamster ovary cells by guanyl diamines
    • Park MH, Wolff EC, Lee YB, Folk JE. Antiproliferative effects of inhibitors of deoxyhypusine synthase. Inhibition of growth of Chinese hamster ovary cells by guanyl diamines. J Biol Chem 1994;269:27827-32
    • (1994) J Biol Chem , vol.269 , pp. 27827-27832
    • Park, M.H.1    Wolff, E.C.2    Lee, Y.B.3    Folk, J.E.4
  • 35
    • 0006806047 scopus 로고    scopus 로고
    • Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae
    • Park MH, Joe YA, Kang KR. Deoxyhypusine synthase activity is essential for cell viability in the yeast Saccharomyces cerevisiae. J Biol Chem 1998;273:1677-83
    • (1998) J Biol Chem , vol.273 , pp. 1677-1683
    • Park, M.H.1    Joe, Y.A.2    Kang, K.R.3
  • 36
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation?
    • Pinna LA. Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim Biophys Acta 1990;1054:267-84
    • (1990) Biochim Biophys Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 37
    • 0037226593 scopus 로고    scopus 로고
    • A molecular signature of metastasis in primary solid tumors
    • Ramaswamy S, Ross KN, Lander ES, Golub TR. A molecular signature of metastasis in primary solid tumors. Nat Genet 2003;33:49-54
    • (2003) Nat Genet , vol.33 , pp. 49-54
    • Ramaswamy, S.1    Ross, K.N.2    Lander, E.S.3    Golub, T.R.4
  • 38
    • 0030000577 scopus 로고    scopus 로고
    • Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae
    • Sasaki K, Abid MR, Miyazaki M. Deoxyhypusine synthase gene is essential for cell viability in the yeast Saccharomyces cerevisiae. FEBS Lett 1996;384:151-4
    • (1996) FEBS Lett , vol.384 , pp. 151-154
    • Sasaki, K.1    Abid, M.R.2    Miyazaki, M.3
  • 39
    • 0025810272 scopus 로고
    • Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae
    • Schnier J, Schwelberger HG, Smit-McBride Z, Kang HA, Hershey JW. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1991:3105-14
    • (1991) Mol Cell Biol , pp. 3105-3114
    • Schnier, J.1    Schwelberger, H.G.2    Smit-McBride, Z.3    Kang, H.A.4    Hershey, J.W.5
  • 40
    • 0028864613 scopus 로고
    • Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA
    • Tao Y, Chen KY. Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA. J Biol Chem 1995a;270:23984-7
    • (1995) J Biol Chem , vol.270 , pp. 23984-23987
    • Tao, Y.1    Chen, K.Y.2
  • 41
    • 0028859315 scopus 로고
    • Purification of deoxyhypusine synthase from Neurospora crassa to homogeneity by substrate elution affinity chromatography
    • Tao Y, Chen KY. Purification of deoxyhypusine synthase from Neurospora crassa to homogeneity by substrate elution affinity chromatography. J Biol Chem 1995b;270:383-6
    • (1995) J Biol Chem , vol.270 , pp. 383-386
    • Tao, Y.1    Chen, K.Y.2
  • 42
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnology 1992;24:145-9
    • (1992) Biotechnology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 43
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter JC, Adams MD, Myers EW, et al. The sequence of the human genome. Science 2001;291:1304-51
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1    Adams, M.D.2    Myers, E.W.3
  • 44
    • 0027485617 scopus 로고
    • The HYP2 gene of Saccharomyces cerevisiae is essential for aerobic growth: Characterization of different isoforms of the hypusine-containing protein Hyp2p and analysis of gene disruption mutants
    • Whl T, Klier H, Ammer H, Lottspeich F, Magdolen V. The HYP2 gene of Saccharomyces cerevisiae is essential for aerobic growth: characterization of different isoforms of the hypusine-containing protein Hyp2p and analysis of gene disruption mutants. Mol Gen Genet 1993;241:305-11
    • (1993) Mol Gen Genet , vol.241 , pp. 305-311
    • Whl, T.1    Klier, H.2    Ammer, H.3    Lottspeich, F.4    Magdolen, V.5
  • 45
    • 0025264297 scopus 로고
    • Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD
    • Wolff EC, Park MH, Folk JE. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD. J Biol Chem 1990;265:4793-9
    • (1990) J Biol Chem , vol.265 , pp. 4793-4799
    • Wolff, E.C.1    Park, M.H.2    Folk, J.E.3
  • 46
    • 0028965712 scopus 로고
    • Deoxyhypusine synthase from rat testis: Purification and characterization
    • Wolff EC, Lee YB, Chung SI, Folk JE, Park MH. Deoxyhypusine synthase from rat testis: purification and characterization. J Biol Chem 1995;270:8660-6
    • (1995) J Biol Chem , vol.270 , pp. 8660-8666
    • Wolff, E.C.1    Lee, Y.B.2    Chung, S.I.3    Folk, J.E.4    Park, M.H.5
  • 47
    • 0033554888 scopus 로고    scopus 로고
    • Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation
    • Wolff EC, Park MH. Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation. Yeast 1999;15:43-50
    • (1999) Yeast , vol.15 , pp. 43-50
    • Wolff, E.C.1    Park, M.H.2


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