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Volumn 313, Issue 3, 2004, Pages 587-593

Perturbation of ATP-induced tetramerization of human cytosolic thymidine kinase by substitution of serine-13 with aspartic acid at the mitotic phosphorylation site

Author keywords

Cell cycle; Kinetics; Oligomerization; Phosphorylation; Thymidine kinase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; SERINE DERIVATIVE; TETRAMER; THYMIDINE KINASE;

EID: 0347694727     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.147     Document Type: Article
Times cited : (19)

References (29)
  • 1
    • 0016147460 scopus 로고
    • Regulation of thymidine kinase synthesis in human cells
    • Bello L.J. Regulation of thymidine kinase synthesis in human cells. Exp. Cell Res. 89:1974;263-274.
    • (1974) Exp. Cell Res. , vol.89 , pp. 263-274
    • Bello, L.J.1
  • 2
    • 0019988178 scopus 로고
    • Regulation of thymidine kinase enzyme level in serum-stimulated mouse 3T6 fibroblasts
    • Johnson L.F., Rao L.G., Muench A.J. Regulation of thymidine kinase enzyme level in serum-stimulated mouse 3T6 fibroblasts. Exp. Cell Res. 138:1982;79-85.
    • (1982) Exp. Cell Res. , vol.138 , pp. 79-85
    • Johnson, L.F.1    Rao, L.G.2    Muench, A.J.3
  • 3
    • 0016253656 scopus 로고
    • Expression of thymidine kinase variants is a function of the replicative state of cells
    • Adler R., McAuslan B.R. Expression of thymidine kinase variants is a function of the replicative state of cells. Cell. 2:1974;113-117.
    • (1974) Cell , vol.2 , pp. 113-117
    • Adler, R.1    McAuslan, B.R.2
  • 4
    • 0017715352 scopus 로고
    • Induction of thymidine kinases in phytohaemagglutinin-stimulated human lymphocytes
    • Munch-Petersen B., Tyrsted G. Induction of thymidine kinases in phytohaemagglutinin-stimulated human lymphocytes. Biochim. Biophys. Acta. 478:1977;364-375.
    • (1977) Biochim. Biophys. Acta , vol.478 , pp. 364-375
    • Munch-Petersen, B.1    Tyrsted, G.2
  • 5
    • 0021992778 scopus 로고
    • Induction of cellular thymidine kinase occurs at the mRNA level
    • Stuart P., Ito M., Stewart C., Conrad S.E. Induction of cellular thymidine kinase occurs at the mRNA level. Mol. Cell. Biol. 5:1985;1490-1497.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1490-1497
    • Stuart, P.1    Ito, M.2    Stewart, C.3    Conrad, S.E.4
  • 6
    • 0023395549 scopus 로고
    • Control of thymidine kinase mRNA during the cell cycle
    • Coppock D.L., Pardee A.B. Control of thymidine kinase mRNA during the cell cycle. Mol. Cell. Biol. 7:1987;2925-2932.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2925-2932
    • Coppock, D.L.1    Pardee, A.B.2
  • 7
    • 0025195812 scopus 로고
    • Identification of a G1-S-phase-regulated region in the human thymidine kinase gene promoter
    • Roehl H.H., Conrad S.E. Identification of a G1-S-phase-regulated region in the human thymidine kinase gene promoter. Mol. Cell. Biol. 10:1990;3834-3837.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3834-3837
    • Roehl, H.H.1    Conrad, S.E.2
  • 8
    • 0024415487 scopus 로고
    • S-phase-specific regulation by deletion mutants of the human thymidine kinase promoter
    • Lipson K.E., Chen S.T., Koniecki J., Ku D.H., Baserga R. S-phase-specific regulation by deletion mutants of the human thymidine kinase promoter. Proc. Natl. Acad. Sci. USA. 86:1989;6848-6852.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6848-6852
    • Lipson, K.E.1    Chen, S.T.2    Koniecki, J.3    Ku, D.H.4    Baserga, R.5
  • 9
    • 0026069218 scopus 로고
    • Identification of a 70-base-pair cell cycle regulatory unit within the promoter of the human thymidine kinase gene and its interaction with cellular factors
    • Kim Y.K., Lee A.S. Identification of a 70-base-pair cell cycle regulatory unit within the promoter of the human thymidine kinase gene and its interaction with cellular factors. Mol. Cell. Biol. 11:1991;2296-2302.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2296-2302
    • Kim, Y.K.1    Lee, A.S.2
  • 10
    • 0023951483 scopus 로고
    • Regulation of human thymidine kinase during the cell cycle
    • Sherley J.L., Kelly T.J. Regulation of human thymidine kinase during the cell cycle. J. Biol. Chem. 263:1988;8350-8358.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8350-8358
    • Sherley, J.L.1    Kelly, T.J.2
  • 11
    • 0025246151 scopus 로고
    • Independent regulation of thymidine kinase mRNA and enzyme levels in serum-stimulated cells
    • Ito M., Conrad S.E. Independent regulation of thymidine kinase mRNA and enzyme levels in serum-stimulated cells. J. Biol. Chem. 265:1990;6954-6960.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6954-6960
    • Ito, M.1    Conrad, S.E.2
  • 12
    • 0026315964 scopus 로고
    • Cell cycle regulation of thymidine kinase: Residues near the carboxyl terminus are essential for the specific degradation of the enzyme at mitosis
    • Kauffman M.G., Kelly T.J. Cell cycle regulation of thymidine kinase: residues near the carboxyl terminus are essential for the specific degradation of the enzyme at mitosis. Mol. Cell. Biol. 11:1991;2538-2546.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2538-2546
    • Kauffman, M.G.1    Kelly, T.J.2
  • 13
    • 0029889149 scopus 로고    scopus 로고
    • Carboxy-terminal residues of mouse thymidine kinase are essential for rapid degradation in quiescent cells
    • Sutterluety H., Bartl S., Karlseder J., Wintersberger E., Seiser C. Carboxy-terminal residues of mouse thymidine kinase are essential for rapid degradation in quiescent cells. J. Mol. Biol. 259:1996;383-392.
    • (1996) J. Mol. Biol. , vol.259 , pp. 383-392
    • Sutterluety, H.1    Bartl, S.2    Karlseder, J.3    Wintersberger, E.4    Seiser, C.5
  • 14
    • 0027185675 scopus 로고
    • Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties
    • Munch-Petersen B., Tyrsted G., Cloos L. Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties. J. Biol. Chem. 268:1993;15621-15625.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15621-15625
    • Munch-Petersen, B.1    Tyrsted, G.2    Cloos, L.3
  • 16
    • 0027396752 scopus 로고
    • The regulation of thymidine kinase in HL-60 human promyeloleukemia cells
    • Chang Z.F., Huang D.Y. The regulation of thymidine kinase in HL-60 human promyeloleukemia cells. J. Biol. Chem. 268:1993;1266-1271.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1266-1271
    • Chang, Z.F.1    Huang, D.Y.2
  • 17
    • 0029995291 scopus 로고    scopus 로고
    • Existence of phosphorylated and dephosphorylated forms of cytosolic thymidine kinase (TK1)
    • He Q., Skog S., Wu C., Johansson A., Tribukait B. Existence of phosphorylated and dephosphorylated forms of cytosolic thymidine kinase (TK1). Biochim. Biophys. Acta. 1289:1996;25-30.
    • (1996) Biochim. Biophys. Acta , vol.1289 , pp. 25-30
    • He, Q.1    Skog, S.2    Wu, C.3    Johansson, A.4    Tribukait, B.5
  • 18
    • 0028087601 scopus 로고
    • Differential phosphorylation of human thymidine kinase in proliferating and M phase-arrested human cells
    • Chang Z.F., Huang D.Y., Hsue N.C. Differential phosphorylation of human thymidine kinase in proliferating and M phase-arrested human cells. J. Biol. Chem. 269:1994;21249-21254.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21249-21254
    • Chang, Z.F.1    Huang, D.Y.2    Hsue, N.C.3
  • 19
    • 0032524346 scopus 로고    scopus 로고
    • Serine 13 is the site of mitotic phosphorylation of human thymidine kinase
    • Chang Z.F., Huang D.Y., Chi L.M. Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J. Biol. Chem. 273:1998;12095-12100.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12095-12100
    • Chang, Z.F.1    Huang, D.Y.2    Chi, L.M.3
  • 20
    • 0034644693 scopus 로고    scopus 로고
    • Valine, not methionine, is amino acid 106 in human cytosolic thymidine kinase (TK1). Impact on oligomerization, stability, and kinetic properties
    • Berenstein D., Christensen J.F., Kristensen T., Hofbauer R., Munch-Petersen B. Valine, not methionine, is amino acid 106 in human cytosolic thymidine kinase (TK1). Impact on oligomerization, stability, and kinetic properties. J. Biol. Chem. 275:2000;32187-32192.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32187-32192
    • Berenstein, D.1    Christensen, J.F.2    Kristensen, T.3    Hofbauer, R.4    Munch-Petersen, B.5
  • 21
    • 0037443087 scopus 로고    scopus 로고
    • Degradation of human thymidine kinase is dependent on serine-13 phosphorylation: Involvement of the SCF-mediated pathway
    • Ke P.Y., Yang C.C., Tsai I.C., Chang Z.F. Degradation of human thymidine kinase is dependent on serine-13 phosphorylation: involvement of the SCF-mediated pathway. Biochem. J. 370:2003;265-273.
    • (2003) Biochem. J. , vol.370 , pp. 265-273
    • Ke, P.Y.1    Yang, C.C.2    Tsai, I.C.3    Chang, Z.F.4
  • 22
    • 0035963547 scopus 로고    scopus 로고
    • ′ -untranslated region of human thymidine kinase mRNA
    • ′ -untranslated region of human thymidine kinase mRNA Biochim. Biophys. Acta. 1519:2001;209-215.
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 209-215
    • Chou, W.L.1    Chang, Z.F.2
  • 23
    • 0021741979 scopus 로고
    • Differences in the kinetic properties of thymidine kinase isoenzymes in unstimulated and phytohemagglutinin-stimulated human lymphocytes
    • Munch-Petersen B. Differences in the kinetic properties of thymidine kinase isoenzymes in unstimulated and phytohemagglutinin-stimulated human lymphocytes. Mol. Cell. Biochem. 64:1984;173-185.
    • (1984) Mol. Cell. Biochem. , vol.64 , pp. 173-185
    • Munch-Petersen, B.1
  • 24
    • 0025916482 scopus 로고
    • Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides
    • Munch-Petersen B., Cloos L., Tyrsted G., Eriksson S. Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides. J. Biol. Chem. 266:1991;9032-9038.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9032-9038
    • Munch-Petersen, B.1    Cloos, L.2    Tyrsted, G.3    Eriksson, S.4
  • 25
    • 0034647413 scopus 로고    scopus 로고
    • Substrate binding is a prerequisite for stabilisation of mouse thymidine kinase in proliferating fibroblasts
    • Posch M., Hauser C., Seiser C. Substrate binding is a prerequisite for stabilisation of mouse thymidine kinase in proliferating fibroblasts. J. Mol. Biol. 300:2000;493-502.
    • (2000) J. Mol. Biol. , vol.300 , pp. 493-502
    • Posch, M.1    Hauser, C.2    Seiser, C.3
  • 26
    • 0021742269 scopus 로고
    • Human thymidine kinase gene: Molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells
    • Bradshaw H.D. Jr., Deininger P.L. Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol. Cell. Biol. 4:1984;2316-2320.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2316-2320
    • Bradshaw, H.D.Jr.1    Deininger, P.L.2
  • 27
    • 0018826504 scopus 로고
    • Thymidine concentrations in human sera: Variations in patients with leukaemia and megaloblastic anaemia
    • Holden L., Hoffbrand A.V., Tattersall M.H. Thymidine concentrations in human sera: variations in patients with leukaemia and megaloblastic anaemia. Eur. J. Cancer. 16:1980;115-121.
    • (1980) Eur. J. Cancer , vol.16 , pp. 115-121
    • Holden, L.1    Hoffbrand, A.V.2    Tattersall, M.H.3
  • 28
    • 0026711076 scopus 로고
    • Deoxynucleotide pools and DNA synthesis in resting and PHA-stimulated human lymphocytes treated with mutagens
    • Ferraro P., Bianchi V., Biasin M.R., Celotti L. Deoxynucleotide pools and DNA synthesis in resting and PHA-stimulated human lymphocytes treated with mutagens. Exp. Cell Res. 199:1992;349-354.
    • (1992) Exp. Cell Res. , vol.199 , pp. 349-354
    • Ferraro, P.1    Bianchi, V.2    Biasin, M.R.3    Celotti, L.4
  • 29
    • 0347986676 scopus 로고    scopus 로고
    • Mitotic degradation of human thymidine kinase 1 is dependent on APC/Cdh1 pathway
    • in press
    • P.Y. Ke, Z.F. Chang, Mitotic degradation of human thymidine kinase 1 is dependent on APC/Cdh1 pathway, Mol. Cell. Biol. 24 (2004), in press.
    • (2004) Mol. Cell. Biol. , vol.24
    • Ke, P.Y.1    Chang, Z.F.2


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