메뉴 건너뛰기




Volumn 191, Issue 1-2, 1999, Pages 97-104

Association of protein kinase CK2 with eukaryotic translation initiation factor eIF-2 and with grp94/ endoplasmin

Author keywords

Calreticulin; Eukaryotic translation initation factor eIF 2; grp94 endoplasmin; Protein kinase CK2; Protein phosphorylation; Rat tissues

Indexed keywords

ANTIBODY; CALRETICULIN; INITIATION FACTOR 2; PROTEIN KINASE;

EID: 0033064008     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-1-4419-8624-5_12     Document Type: Article
Times cited : (24)

References (33)
  • 1
    • 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 1054: 267-284, 1990
    • (1990) Biochim Biophys Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 2
    • 0027430998 scopus 로고
    • Casein kinases: Pleiotropic mediators of cellular regulation
    • Issinger O-G: Casein kinases: Pleiotropic mediators of cellular regulation. Pharmac Ther 59: 1-30, 1993
    • (1993) Pharmac Ther , vol.59 , pp. 1-30
    • Issinger, O.-G.1
  • 3
    • 0028985936 scopus 로고
    • Casein kinase IIα transgen-induced murine lymphoma: Relation to theileriosis in cattle
    • Seldin DC, Leder P: Casein kinase IIα transgen-induced murine lymphoma: Relation to theileriosis in cattle. Science 267: 894-896, 1995
    • (1995) Science , vol.267 , pp. 894-896
    • Seldin, D.C.1    Leder, P.2
  • 4
    • 0029019790 scopus 로고
    • Interactions between the subunits of casein kinase II
    • Gietz DR, Graham KC, Litchfield DW: Interactions between the subunits of casein kinase II. J Biol Chem 270: 13017-13021, 1995
    • (1995) J Biol Chem , vol.270 , pp. 13017-13021
    • Gietz, D.R.1    Graham, K.C.2    Litchfield, D.W.3
  • 6
    • 0028265483 scopus 로고
    • Biosynthesis of casein kinase II in lymphoid cells
    • Lüscher B, Litchfield DW: Biosynthesis of casein kinase II in lymphoid cells. Eur J Biochem 220: 521-526, 1994
    • (1994) Eur J Biochem , vol.220 , pp. 521-526
    • Lüscher, B.1    Litchfield, D.W.2
  • 7
    • 0027715235 scopus 로고
    • A majority of casein kinase II α subunit is tightly bound to intranuclear components but not to the β subunit
    • Stigare J, Buddelmeijer N, Egyhazi E: A majority of casein kinase II α subunit is tightly bound to intranuclear components but not to the β subunit. Mol Cell Biochem 129: 77-85, 1993
    • (1993) Mol Cell Biochem , vol.129 , pp. 77-85
    • Stigare, J.1    Buddelmeijer, N.2    Egyhazi, E.3
  • 8
    • 0031056967 scopus 로고    scopus 로고
    • The regulatory subunit of protein kinase CK2 is a specific A-Raf activator
    • Hagemann C, Kalmes A, Wixler V, Schuster T, Rapp UR: The regulatory subunit of protein kinase CK2 is a specific A-Raf activator. FEBS Lett 403: 200-202, 1997
    • (1997) FEBS Lett , vol.403 , pp. 200-202
    • Hagemann, C.1    Kalmes, A.2    Wixler, V.3    Schuster, T.4    Rapp, U.R.5
  • 9
    • 0030948574 scopus 로고    scopus 로고
    • The casein kinase II beta subunit binds to Mos and inhibits Mos activity
    • Chen K, Li D, Krebs EG, Cooper JA: The casein kinase II beta subunit binds to Mos and inhibits Mos activity. Mol Cell Biol 4: 1904-1912, 1997
    • (1997) Mol Cell Biol , vol.4 , pp. 1904-1912
    • Chen, K.1    Li, D.2    Krebs, E.G.3    Cooper, J.A.4
  • 10
    • 0031050906 scopus 로고    scopus 로고
    • A-Raf is a new interacting partner of protein kinase CK2β subunit
    • Boldyreff B, Issinger O-G: A-Raf is a new interacting partner of protein kinase CK2β subunit. FEBS Lett 403: 197-199, 1997
    • (1997) FEBS Lett , vol.403 , pp. 197-199
    • Boldyreff, B.1    Issinger, O.-G.2
  • 12
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Myata Y, Yahara I: The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J Biol Chem 267: 7042-7047, 1992
    • (1992) J Biol Chem , vol.267 , pp. 7042-7047
    • Myata, Y.1    Yahara, I.2
  • 13
    • 0027433079 scopus 로고
    • DNA topoisomerase II and casein kinase II associate in a molecular complex that is catalytically active
    • Bojanowski K, Filhol O, Cochet C, Chambaz EM, Larsen A-K: DNA topoisomerase II and casein kinase II associate in a molecular complex that is catalytically active. J Biol Chem 268: 22920-22926, 1993
    • (1993) J Biol Chem , vol.268 , pp. 22920-22926
    • Bojanowski, K.1    Filhol, O.2    Cochet, C.3    Chambaz, E.M.4    Larsen, A.-K.5
  • 14
    • 0026673798 scopus 로고
    • Casein kinase II and the tumor suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation
    • Filhol O, Baudier J, Delphin C, Loue-Mackenbach P, Chambaz EM, Cochet C: Casein kinase II and the tumor suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation. J Biol Chem 267: 20577-20583, 1992
    • (1992) J Biol Chem , vol.267 , pp. 20577-20583
    • Filhol, O.1    Baudier, J.2    Delphin, C.3    Loue-Mackenbach, P.4    Chambaz, E.M.5    Cochet, C.6
  • 15
    • 0029900546 scopus 로고    scopus 로고
    • The physical association of casein kinase 2 with nucleolin
    • Li D, Dobrowolska G, Krebs EG: The physical association of casein kinase 2 with nucleolin. J Biol Chem 271: 15662-15668, 1996
    • (1996) J Biol Chem , vol.271 , pp. 15662-15668
    • Li, D.1    Dobrowolska, G.2    Krebs, E.G.3
  • 16
    • 0028863946 scopus 로고
    • A casein-kinase-2-related protein kinase is tightly associated with the large antigen of simian virus 40
    • Götz C, Koenig MG, Issinger O-G, Montenarh M: A casein-kinase-2-related protein kinase is tightly associated with the large antigen of simian virus 40. FEBS Lett 233: 327-334, 1995
    • (1995) FEBS Lett , vol.233 , pp. 327-334
    • Götz, C.1    Koenig, M.G.2    Issinger, O.-G.3    Montenarh, M.4
  • 17
    • 0031047830 scopus 로고    scopus 로고
    • Casein kinase II binds and phosphorylates cytoplasmic dynein
    • Karki S, Tokito M, Holzbaur ELF: Casein kinase II binds and phosphorylates cytoplasmic dynein. J Biol Chem 272: 5887-5891, 1997
    • (1997) J Biol Chem , vol.272 , pp. 5887-5891
    • Karki, S.1    Tokito, M.2    Elf, H.3
  • 18
    • 0031013280 scopus 로고    scopus 로고
    • Specific interaction between casein kinase 2 and the nucleolar protein Nopp 140
    • Li D, Meier T, Dobrowolska G, Krebs EG: Specific interaction between casein kinase 2 and the nucleolar protein Nopp 140. J Biol Chem 272: 3773-3779, 1997
    • (1997) J Biol Chem , vol.272 , pp. 3773-3779
    • Li, D.1    Meier, T.2    Dobrowolska, G.3    Krebs, E.G.4
  • 19
    • 0030973456 scopus 로고    scopus 로고
    • Casein kinase 2 associates with and phosphorylates Dishevelled
    • Willert K, Brink M, Wodarz A, Varmus H, Nusse R: Casein kinase 2 associates with and phosphorylates Dishevelled. EMBO J 16: 3089-3096, 1997
    • (1997) EMBO J , vol.16 , pp. 3089-3096
    • Willert, K.1    Brink, M.2    Wodarz, A.3    Varmus, H.4    Nusse, R.5
  • 20
    • 0025871855 scopus 로고
    • Heterogeneity of rat liver cytosol casein kinase 2
    • Molina E, Plana M, Itarte E: Heterogeneity of rat liver cytosol casein kinase 2. Biochem J 277: 811-818, 1991
    • (1991) Biochem J , vol.277 , pp. 811-818
    • Molina, E.1    Plana, M.2    Itarte, E.3
  • 21
    • 2142781320 scopus 로고    scopus 로고
    • Rat liver pp49, a protein that forms complexes with protein kinase CK2, is composed of the β and the γ subunits of translation initiation factor eIF-2
    • Gil C, Plana M, Riera M, Itarte E: Rat liver pp49, a protein that forms complexes with protein kinase CK2, is composed of the β and the γ subunits of translation initiation factor eIF-2. Biochem Biophys Res Commun 225: 1052-1057, 1996
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 1052-1057
    • Gil, C.1    Plana, M.2    Riera, M.3    Itarte, E.4
  • 22
    • 0031213762 scopus 로고    scopus 로고
    • Substrates for protein kinase CK2 in insulin receptor preparations from rat liver membranes: Identification of a 210-kDa protein substrate as the dimeric form of endoplasmin
    • Trujillo R, Miró F, Plana M, José M, Bollen M, Stalmans W, Itarte E: Substrates for protein kinase CK2 in insulin receptor preparations from rat liver membranes: Identification of a 210-kDa protein substrate as the dimeric form of endoplasmin. Arch Biochem Biophys 344: 18-28, 1997
    • (1997) Arch Biochem Biophys , vol.344 , pp. 18-28
    • Trujillo, R.1    Miró, F.2    Plana, M.3    José, M.4    Bollen, M.5    Stalmans, W.6    Itarte, E.7
  • 23
    • 0022249124 scopus 로고
    • Glycogen synthase (casein) kinase-1: Tissue distribution and subcellular localization
    • Singh TJ, Huang K-P: Glycogen synthase (casein) kinase-1: Tissue distribution and subcellular localization. FEBS Lett 190: 84-88, 1985
    • (1985) FEBS Lett , vol.190 , pp. 84-88
    • Singh, T.J.1    Huang, K.-P.2
  • 24
    • 0028251136 scopus 로고
    • Distribution of MAP kinase, S6 kinase, and casein kinase II in rat tissues: Activation by insulin in spleen
    • Hei YH, Chen X, Diamond J, McNeill JH: Distribution of MAP kinase, S6 kinase, and casein kinase II in rat tissues: Activation by insulin in spleen. Biochem Cell Biol 72: 49-53, 1994
    • (1994) Biochem Cell Biol , vol.72 , pp. 49-53
    • Hei, Y.H.1    Chen, X.2    Diamond, J.3    McNeill, J.H.4
  • 25
    • 0021099528 scopus 로고
    • Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis
    • Duncan R, Hershey JWB: Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem 258: 7228-7235, 1983
    • (1983) J Biol Chem , vol.258 , pp. 7228-7235
    • Duncan, R.1    Hershey, J.2
  • 26
    • 0028203337 scopus 로고
    • Use of monoclonal antibodies to study the estructure and function of eukaryotic protein synthesis initiation factor eIF-2B
    • Oldfield S, Jones BL, Tanton D, Proud CG: Use of monoclonal antibodies to study the estructure and function of eukaryotic protein synthesis initiation factor eIF-2B. Eur J Biochem 221: 399-410, 1994
    • (1994) Eur J Biochem , vol.221 , pp. 399-410
    • Oldfield, S.1    Jones, B.L.2    Tanton, D.3    Proud, C.G.4
  • 27
    • 0024338805 scopus 로고
    • The two forms of the β-subunit of initiation factor-2 from reticolocyte lysates arise from proteolytic degradation
    • Price NT, Nakielny SF, Clark SJ, Proud CG: The two forms of the β-subunit of initiation factor-2 from reticolocyte lysates arise from proteolytic degradation. Biochim Biophys Acta 1008: 177-182, 1989
    • (1989) Biochim Biophys Acta , vol.1008 , pp. 177-182
    • Price, N.T.1    Nakielny, S.F.2    Clark, S.J.3    Proud, C.G.4
  • 28
    • 0031054687 scopus 로고    scopus 로고
    • Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenin nucleotide-independent
    • Wearsch P, Nicchitta CV: Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenin nucleotide-independent. J Biol Chem 272: 5152-5156, 1997
    • (1997) J Biol Chem , vol.272 , pp. 5152-5156
    • Wearsch, P.1    Nicchitta, C.V.2
  • 29
    • 0030567964 scopus 로고    scopus 로고
    • Identification of glycyrrhizin-binding protein kinase as casein kinase II and characterization of its associated phosphate acceptors in mouse liver
    • Harada S, Karino A, Shimoyama Y, Shamsa F, Ohtuski K: Identification of glycyrrhizin-binding protein kinase as casein kinase II and characterization of its associated phosphate acceptors in mouse liver. Biochem Biophys Res Commun 227: 102-109, 1996
    • (1996) Biochem Biophys Res Commun , vol.227 , pp. 102-109
    • Harada, S.1    Karino, A.2    Shimoyama, Y.3    Shamsa, F.4    Ohtuski, K.5
  • 30
    • 0029989731 scopus 로고    scopus 로고
    • Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2
    • Baldan B, Navazio L, Firso A, Mariani P, Meggio F: Plant calreticulin is specifically and efficiently phosphorylated by protein kinase CK2. Biochem Biophys Res Commun 221: 498-502, 1996
    • (1996) Biochem Biophys Res Commun , vol.221 , pp. 498-502
    • Baldan, B.1    Navazio, L.2    Firso, A.3    Mariani, P.4    Meggio, F.5
  • 33
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • Proud CG: Protein phosphorylation in translational control. Curr Top Cell Reg 32: 243-369, 1992
    • (1992) Curr Top Cell Reg , vol.32 , pp. 243-369
    • Proud, C.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.