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Volumn 63, Issue 7-8, 2006, Pages 781-795

Protein kinases controlling the onset of mitosis

Author keywords

Checkpoint; DNA damage; Mitosis; Phosphorylation; Protein kinase structure

Indexed keywords

AURORA A KINASE; AURORA B KINASE; CYCLIN DEPENDENT KINASE 1; NEK2 PROTEIN; POLO LIKE KINASE 1; PROTEIN; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 33646573938     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5515-3     Document Type: Review
Times cited : (49)

References (192)
  • 1
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • Burnett G. and Kennedy E. P. (1954) The enzymatic phosphorylation of proteins. J. Biol. Chem. 211: 969-980
    • (1954) J. Biol. Chem. , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 2
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • Fischer E. H. and Krebs E. G. (1955) Conversion of phosphorylase b to phosphorylase a in muscle extracts. J. Biol. Chem. 216: 121-132
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 3
    • 0001268037 scopus 로고
    • Inactivation and activation of liver phosphorylase
    • Sutherland E. W. Jr and Wosilait W. D. (1955) Inactivation and activation of liver phosphorylase. Nature 175: 169-170
    • (1955) Nature , vol.175 , pp. 169-170
    • Sutherland Jr., E.W.1    Wosilait, W.D.2
  • 4
    • 70449285205 scopus 로고
    • Factors affecting the activity of muscle phosphorylase b kinase
    • Krebs E. G., Graves D. J. and Fischer E. H. (1959) Factors affecting the activity of muscle phosphorylase b kinase. J. Biol. Chem. 234: 2867-2873
    • (1959) J. Biol. Chem. , vol.234 , pp. 2867-2873
    • Krebs, E.G.1    Graves, D.J.2    Fischer, E.H.3
  • 5
    • 0642347850 scopus 로고    scopus 로고
    • The mitotic checkpoint: A signaling pathway that allows a single unattached kinetochore to inhibit mitotic exit
    • Chan G. K. and Yen T. J. (2003) The mitotic checkpoint: a signaling pathway that allows a single unattached kinetochore to inhibit mitotic exit. Prog. Cell Cycle Res. 5: 431-439
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 431-439
    • Chan, G.K.1    Yen, T.J.2
  • 6
    • 0036789555 scopus 로고    scopus 로고
    • The spindle checkpoint: Structural insights into dynamic signalling
    • Musacchio A. and Hardwick K. G. (2002) The spindle checkpoint: structural insights into dynamic signalling. Nat. Rev. Mol. Cell. Biol. 3: 731-741
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 731-741
    • Musacchio, A.1    Hardwick, K.G.2
  • 7
    • 18044396994 scopus 로고    scopus 로고
    • Bub1 and the multilayered inhibition of Cdc20-APC/C in mitosis
    • Vanoosthuyse V. and Hardwick K. G. (2005) Bub1 and the multilayered inhibition of Cdc20-APC/C in mitosis. Trends Cell Biol. 15: 231-233
    • (2005) Trends Cell Biol. , vol.15 , pp. 231-233
    • Vanoosthuyse, V.1    Hardwick, K.G.2
  • 8
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks S. K., Quinn A. M. and Hunter T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42-52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 9
    • 0023651349 scopus 로고
    • A thousand and one protein kinases
    • Hunter T. (1987) A thousand and one protein kinases. Cell 50: 823-829
    • (1987) Cell , vol.50 , pp. 823-829
    • Hunter, T.1
  • 10
    • 0038339419 scopus 로고    scopus 로고
    • Genomic analysis of the eukaryotic protein kinase superfamily: A perspective
    • Hanks S. K. (2003) Genomic analysis of the eukaryotic protein kinase superfamily: a perspective. Genome Biol. 4: 111
    • (2003) Genome Biol. , vol.4 , pp. 111
    • Hanks, S.K.1
  • 13
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • Johnson L. N. and Lewis R. J. (2001) Structural basis for control by phosphorylation. Chem. Rev. 101: 2209-2242
    • (2001) Chem. Rev. , vol.101 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 14
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M. and Kuriyan J. (2002) The conformational plasticity of protein kinases. Cell 109: 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 15
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson L. N., Noble M. E. and Owen D. J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell 85: 149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 16
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B., Taylor S. and Ghosh G. (2004) Regulation of protein kinases; controlling activity through activation segment conformation. Mol. Cell 15: 661-675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 17
    • 0035816678 scopus 로고    scopus 로고
    • Involvement of the activation loop of ERK in the detachment from cytosolic anchoring
    • Wolf I., Rubinfeld H., Yoon S., Marmor G., Hanoch T. and Seger R. (2001) Involvement of the activation loop of ERK in the detachment from cytosolic anchoring. J. Biol. Chem. 276: 24490-24497
    • (2001) J. Biol. Chem. , vol.276 , pp. 24490-24497
    • Wolf, I.1    Rubinfeld, H.2    Yoon, S.3    Marmor, G.4    Hanoch, T.5    Seger, R.6
  • 18
    • 0033130136 scopus 로고    scopus 로고
    • A unifying concept: The history of cell theory
    • Mazzarello P. (1999) A unifying concept: the history of cell theory. Nat. Cell Biol. 1: E13-E15
    • (1999) Nat. Cell Biol. , vol.1
    • Mazzarello, P.1
  • 19
    • 0000124997 scopus 로고
    • Ueber die Teilung centrigugierte Eier von Ascaris megalocephala
    • Boveri T. (1910) Ueber die Teilung centrigugierte Eier von Ascaris megalocephala. Wilhelm Roux Arch. Entwicklungsmech. Org. 30: 101-125
    • (1910) Wilhelm Roux Arch. Entwicklungsmech. Org. , vol.30 , pp. 101-125
    • Boveri, T.1
  • 20
    • 1842503941 scopus 로고    scopus 로고
    • Spindle mechanics and dynamics during mitosis in Drosophila
    • Kwon M. and Scholey J. M. (2004) Spindle mechanics and dynamics during mitosis in Drosophila. Trends Cell Biol. 14: 194-205
    • (2004) Trends Cell Biol. , vol.14 , pp. 194-205
    • Kwon, M.1    Scholey, J.M.2
  • 21
    • 0344898246 scopus 로고    scopus 로고
    • Introduction to chromosome dynamics in mitosis
    • Watrin E. and Legagneux V. (2003) Introduction to chromosome dynamics in mitosis. Biol. Cell 95: 507-513
    • (2003) Biol. Cell , vol.95 , pp. 507-513
    • Watrin, E.1    Legagneux, V.2
  • 22
    • 0037349338 scopus 로고    scopus 로고
    • The making of the mitotic chromosome: Modern insights into classical questions
    • Swedlow J. R. and Hirano T. (2003) The making of the mitotic chromosome: modern insights into classical questions. Mol. Cell 11: 557-569
    • (2003) Mol. Cell , vol.11 , pp. 557-569
    • Swedlow, J.R.1    Hirano, T.2
  • 23
    • 13244283007 scopus 로고    scopus 로고
    • The anaphase-promoting complex: A key factor in the regulation of cell cycle
    • Castro A., Bernis C., Vigneron S., Labbe J. C. and Lorca T. (2005) The anaphase-promoting complex: a key factor in the regulation of cell cycle. Oncogene 24: 314-325
    • (2005) Oncogene , vol.24 , pp. 314-325
    • Castro, A.1    Bernis, C.2    Vigneron, S.3    Labbe, J.C.4    Lorca, T.5
  • 24
    • 0035144407 scopus 로고    scopus 로고
    • Re-staging mitosis: A contemporary view of mitotic progression
    • Pines J. and Rieder C. L. (2001) Re-staging mitosis: a contemporary view of mitotic progression. Nat. Cell Biol. 3: E3-E6
    • (2001) Nat. Cell Biol. , vol.3
    • Pines, J.1    Rieder, C.L.2
  • 25
    • 0016793098 scopus 로고
    • Genetic control of cell size at cell division in yeast
    • Nurse P. (1975) Genetic control of cell size at cell division in yeast. Nature 256: 547-551
    • (1975) Nature , vol.256 , pp. 547-551
    • Nurse, P.1
  • 26
    • 0015076873 scopus 로고
    • Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes
    • Masui Y. and Markert C. L. (1971) Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177: 129-145
    • (1971) J. Exp. Zool. , vol.177 , pp. 129-145
    • Masui, Y.1    Markert, C.L.2
  • 27
    • 0015080763 scopus 로고
    • The interaction of steroids with Rana pipiens Oocytes in the induction of maturation
    • Smith L. D. and Ecker R. E. (1971) The interaction of steroids with Rana pipiens Oocytes in the induction of maturation. Dev. Biol. 25: 232-247
    • (1971) Dev. Biol. , vol.25 , pp. 232-247
    • Smith, L.D.1    Ecker, R.E.2
  • 28
    • 0345054420 scopus 로고
    • Purification of maturation-promoting factor, an intracellular regulator of early mitotic events
    • USA
    • Lohka M. J., Hayes M. K. and Maller J. L. (1988) Purification of maturation-promoting factor, an intracellular regulator of early mitotic events. Proc. Natl. Acad. Sci. USA 85: 3009-3013
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 3009-3013
    • Lohka, M.J.1    Hayes, M.K.2    Maller, J.L.3
  • 29
    • 0024299475 scopus 로고
    • Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2+
    • Gautier J., Norbury C., Lohka M., Nurse P. and Maller J. (1988) Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2+. Cell 54: 433-439
    • (1988) Cell , vol.54 , pp. 433-439
    • Gautier, J.1    Norbury, C.2    Lohka, M.3    Nurse, P.4    Maller, J.5
  • 30
    • 0024294002 scopus 로고
    • cdc2 is a component of the M phase-specific histone H1 kinase: Evidence for identity with MPF
    • Arion D., Meijer L., Brizuela L. and Beach D. (1988) cdc2 is a component of the M phase-specific histone H1 kinase: evidence for identity with MPF. Cell 55: 371-378
    • (1988) Cell , vol.55 , pp. 371-378
    • Arion, D.1    Meijer, L.2    Brizuela, L.3    Beach, D.4
  • 31
    • 0023753715 scopus 로고
    • The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis
    • Dunphy W. G., Brizuela L., Beach D. and Newport J. (1988) The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis. Cell 54: 423-431
    • (1988) Cell , vol.54 , pp. 423-431
    • Dunphy, W.G.1    Brizuela, L.2    Beach, D.3    Newport, J.4
  • 32
    • 0023688018 scopus 로고
    • Activation at M-phase of a protein kinase encoded by a starfish homologue of the cell cycle control gene cdc2+
    • Labbe J. C., Lee M. G., Nurse P., Picard A. and Doree M. (1988) Activation at M-phase of a protein kinase encoded by a starfish homologue of the cell cycle control gene cdc2+. Nature 335: 251-254
    • (1988) Nature , vol.335 , pp. 251-254
    • Labbe, J.C.1    Lee, M.G.2    Nurse, P.3    Picard, A.4    Doree, M.5
  • 33
    • 0025012866 scopus 로고
    • Cyclin is a component of maturation-promoting factor from Xenopus
    • Gautier J., Minshull J., Lohka M., Glotzer M., Hunt T. and Maller J. L. (1990) Cyclin is a component of maturation-promoting factor from Xenopus. Cell 60: 487-494
    • (1990) Cell , vol.60 , pp. 487-494
    • Gautier, J.1    Minshull, J.2    Lohka, M.3    Glotzer, M.4    Hunt, T.5    Maller, J.L.6
  • 34
    • 0024342438 scopus 로고
    • MPF from starfish oocytes at first meiotic metaphase is a heterodimer containing one molecule of cdc2 and one molecule of cyclin B
    • Labbe J. C., Capony J. P., Caput D., Cavadore J. C., Derancourt J., Kaghad M. et al. (1989) MPF from starfish oocytes at first meiotic metaphase is a heterodimer containing one molecule of cdc2 and one molecule of cyclin B. EMBO J. 8: 3053-3058
    • (1989) EMBO J. , vol.8 , pp. 3053-3058
    • Labbe, J.C.1    Capony, J.P.2    Caput, D.3    Cavadore, J.C.4    Derancourt, J.5    Kaghad, M.6
  • 35
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D. O. (1995) Principles of CDK regulation. Nature 374: 131-134
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 36
    • 0029079936 scopus 로고
    • Cell cycle regulation of the cyclin A, cdc25C and cdc2 genes is based on a common mechanism of transcriptional repression
    • Zwicker J., Lucibello F. C., Wolfraim L. A., Gross C., Truss M., Engeland K. et al. (1995) Cell cycle regulation of the cyclin A, cdc25C and cdc2 genes is based on a common mechanism of transcriptional repression. EMBO J. 14: 4514-4522
    • (1995) EMBO J. , vol.14 , pp. 4514-4522
    • Zwicker, J.1    Lucibello, F.C.2    Wolfraim, L.A.3    Gross, C.4    Truss, M.5    Engeland, K.6
  • 37
    • 0032553322 scopus 로고    scopus 로고
    • Cell cycle-dependent usage of transcriptional start sites. A novel mechanism for regulation of cyclin B1
    • Hwang A., McKenna W. G. and Muschel R. J. (1998) Cell cycle-dependent usage of transcriptional start sites. A novel mechanism for regulation of cyclin B1. J. Biol. Chem. 273: 31505-31509
    • (1998) J. Biol. Chem. , vol.273 , pp. 31505-31509
    • Hwang, A.1    McKenna, W.G.2    Muschel, R.J.3
  • 38
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey P. D., Russo A. A., Polyak K., Gibbs E., Hurwitz J., Massague J. et al. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 376: 313-320
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1    Russo, A.A.2    Polyak, K.3    Gibbs, E.4    Hurwitz, J.5    Massague, J.6
  • 39
    • 0028856425 scopus 로고
    • MAT1 ('menage a trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK
    • Devault A., Martinez A. M., Fesquet D., Labbe J. C., Morin N., Tassan J. P. et al. (1995) MAT1 ('menage a trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK. EMBO J. 14: 5027-5036
    • (1995) EMBO J. , vol.14 , pp. 5027-5036
    • Devault, A.1    Martinez, A.M.2    Fesquet, D.3    Labbe, J.C.4    Morin, N.5    Tassan, J.P.6
  • 40
    • 0028882228 scopus 로고
    • In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein
    • Tassan J. P., Jaquenoud M., Fry A. M., Frutiger S., Hughes G. J. and Nigg E. A. (1995) in vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J. 14: 5608-5617
    • (1995) EMBO J. , vol.14 , pp. 5608-5617
    • Tassan, J.P.1    Jaquenoud, M.2    Fry, A.M.3    Frutiger, S.4    Hughes, G.J.5    Nigg, E.A.6
  • 41
    • 0026713875 scopus 로고
    • Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15
    • Gu Y., Rosenblatt J. and Morgan D. O. (1992) Cell cycle regulation of CDK2 activity by phosphorylation of Thr160 and Tyr15. EMBO J. 11: 3995-4005
    • (1992) EMBO J. , vol.11 , pp. 3995-4005
    • Gu, Y.1    Rosenblatt, J.2    Morgan, D.O.3
  • 42
    • 0032521196 scopus 로고    scopus 로고
    • T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21
    • Ohta T., Okamoto K., Isohashi F., Shibata K., Fukuda M., Yamaguchi S. et al. (1998) T-loop deletion of CDC2 from breast cancer tissues eliminates binding to cyclin B1 and cyclin-dependent kinase inhibitor p21. Cancer Res. 58: 1095-1098
    • (1998) Cancer Res. , vol.58 , pp. 1095-1098
    • Ohta, T.1    Okamoto, K.2    Isohashi, F.3    Shibata, K.4    Fukuda, M.5    Yamaguchi, S.6
  • 43
    • 0024959919 scopus 로고
    • Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis
    • Gould K. L. and Nurse P. (1989) Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature 342: 39-45
    • (1989) Nature , vol.342 , pp. 39-45
    • Gould, K.L.1    Nurse, P.2
  • 45
    • 0027746003 scopus 로고
    • Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase
    • Izumi T. and Maller J. L. (1993) Elimination of cdc2 phosphorylation sites in the cdc25 phosphatase blocks initiation of M-phase. Mol. Biol. Cell 4: 1337-1350
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1337-1350
    • Izumi, T.1    Maller, J.L.2
  • 46
    • 0028168379 scopus 로고
    • Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis
    • Strausfeld U., Fernandez A., Capony J. P., Girard F., Lautredou N., Derancourt J. et al. (1994) Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis. J. Biol. Chem. 269: 5989-6000
    • (1994) J. Biol. Chem. , vol.269 , pp. 5989-6000
    • Strausfeld, U.1    Fernandez, A.2    Capony, J.P.3    Girard, F.4    Lautredou, N.5    Derancourt, J.6
  • 47
    • 0036256260 scopus 로고    scopus 로고
    • Plk1 promotes nuclear translocation of human Cdc25C during prophase
    • Toyoshima-Morimoto F., Taniguchi E. and Nishida E. (2002) Plk1 promotes nuclear translocation of human Cdc25C during prophase. EMBO Rep. 3: 341-348
    • (2002) EMBO Rep. , vol.3 , pp. 341-348
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Nishida, E.3
  • 49
    • 0023443586 scopus 로고
    • Interaction between cdc13+ and cdc2+ in the control of mitosis in fission yeast: Dissociation of the G1 and G2 roles of the cdc2+ protein kinase
    • Booher R. and Beach D. (1987) Interaction between cdc13+ and cdc2+ in the control of mitosis in fission yeast: dissociation of the G1 and G2 roles of the cdc2+ protein kinase. EMBO J. 6: 3441-3447
    • (1987) EMBO J. , vol.6 , pp. 3441-3447
    • Booher, R.1    Beach, D.2
  • 50
    • 0023647143 scopus 로고
    • Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2
    • Lee M. G. and Nurse P. (1987) Complementation used to clone a human homologue of the fission yeast cell cycle control gene cdc2. Nature 327: 31-35
    • (1987) Nature , vol.327 , pp. 31-35
    • Lee, M.G.1    Nurse, P.2
  • 51
    • 0025168713 scopus 로고
    • Drosophila cdc2 homologs: A functional homolog is coexpressed with a cognate variant
    • Lehner C. F. and O'Farrell P. H. (1990) Drosophila cdc2 homologs: a functional homolog is coexpressed with a cognate variant. EMBO J. 9: 3573-3581
    • (1990) EMBO J. , vol.9 , pp. 3573-3581
    • Lehner, C.F.1    O'Farrell, P.H.2
  • 52
    • 0025831974 scopus 로고
    • Evidence that the G1-S and G2-M transitions are controlled by different cdc2 proteins in higher eukaryotes
    • Fang F. and Newport J. W. (1991) Evidence that the G1-S and G2-M transitions are controlled by different cdc2 proteins in higher eukaryotes. Cell 66: 731-742
    • (1991) Cell , vol.66 , pp. 731-742
    • Fang, F.1    Newport, J.W.2
  • 53
    • 0025946804 scopus 로고
    • Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation
    • USA
    • Ninomiya-Tsuji J., Nomoto S., Yasuda H., Reed S. I. and Matsumoto K. (1991) Cloning of a human cDNA encoding a CDC2-related kinase by complementation of a budding yeast cdc28 mutation. Proc. Natl. Acad. Sci. USA 88: 9006-9010
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 9006-9010
    • Ninomiya-Tsuji, J.1    Nomoto, S.2    Yasuda, H.3    Reed, S.I.4    Matsumoto, K.5
  • 54
    • 0024573538 scopus 로고
    • The cdc2 kinase is a nuclear protein that is essential for mitosis in mammalian cells
    • Riabowol K., Draetta G., Brizuela L., Vandre D. and Beach D. (1989) The cdc2 kinase is a nuclear protein that is essential for mitosis in mammalian cells. Cell 57: 393-401
    • (1989) Cell , vol.57 , pp. 393-401
    • Riabowol, K.1    Draetta, G.2    Brizuela, L.3    Vandre, D.4    Beach, D.5
  • 55
    • 0025931223 scopus 로고
    • Okadaic acid mimics a nuclear component required for cyclin B-cdc2 kinase microinjection to drive starfish oocytes into M phase
    • Picard A., Labbe J. C., Barakat H., Cavadore J. C. and Doree M. (1991) Okadaic acid mimics a nuclear component required for cyclin B-cdc2 kinase microinjection to drive starfish oocytes into M phase. J. Cell Biol. 115: 337-344
    • (1991) J. Cell Biol. , vol.115 , pp. 337-344
    • Picard, A.1    Labbe, J.C.2    Barakat, H.3    Cavadore, J.C.4    Doree, M.5
  • 56
    • 0027742184 scopus 로고
    • Distinct roles for cyclin-dependent kinases in cell cycle control
    • van den Heuvel S. and Harlow E. (1993) Distinct roles for cyclin-dependent kinases in cell cycle control. Science 262: 2050-2054
    • (1993) Science , vol.262 , pp. 2050-2054
    • Van Den Heuvel, S.1    Harlow, E.2
  • 57
    • 0032553485 scopus 로고    scopus 로고
    • Requirement for p53 and p21 to sustain G2 arrest after DNA damage
    • Bunz F., Dutriaux A., Lengauer C., Waldman T., Zhou S., Brown J. P. et al. (1998) Requirement for p53 and p21 to sustain G2 arrest after DNA damage. Science 282: 1497-1501
    • (1998) Science , vol.282 , pp. 1497-1501
    • Bunz, F.1    Dutriaux, A.2    Lengauer, C.3    Waldman, T.4    Zhou, S.5    Brown, J.P.6
  • 58
    • 0028899480 scopus 로고
    • Separate domains of p21 involved in the inhibition of Cdk kinase and PCNA
    • Chen J., Jackson P. K., Kirschner M. W. and Dutta A. (1995) Separate domains of p21 involved in the inhibition of Cdk kinase and PCNA. Nature 374: 386-388
    • (1995) Nature , vol.374 , pp. 386-388
    • Chen, J.1    Jackson, P.K.2    Kirschner, M.W.3    Dutta, A.4
  • 59
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • Knockaert M., Greengard P. and Meijer L. (2002) Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol. Sci. 23: 417-425
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 60
    • 0035235736 scopus 로고    scopus 로고
    • Mitotic kinases as regulators of cell division and its checkpoints
    • Nigg E. A. (2001) Mitotic kinases as regulators of cell division and its checkpoints. Nat. Rev. Mol. Cell. Biol. 2: 21-32
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 21-32
    • Nigg, E.A.1
  • 61
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter M., Heitlinger E., Haner M., Aebi U. and Nigg E. A. (1991) Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J. 10: 1535-1544
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Haner, M.3    Aebi, U.4    Nigg, E.A.5
  • 62
    • 0029417238 scopus 로고
    • Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo
    • Blangy A., Lane H. A., d'Herin P., Harper M., Kress M. and Nigg E. A. (1995) Phosphorylation by p34cdc2 regulates spindle association of human Eg5, a kinesin-related motor essential for bipolar spindle formation in vivo. Cell 83: 1159-1169
    • (1995) Cell , vol.83 , pp. 1159-1169
    • Blangy, A.1    Lane, H.A.2    D'Herin, P.3    Harper, M.4    Kress, M.5    Nigg, E.A.6
  • 63
    • 0032538511 scopus 로고    scopus 로고
    • Phosphorylation and activation of 13S condensin by Cdc2 in vitro
    • Kimura K., Hirano M., Kobayashi R. and Hirano T. (1998) Phosphorylation and activation of 13S condensin by Cdc2 in vitro. Science 282: 487-490
    • (1998) Science , vol.282 , pp. 487-490
    • Kimura, K.1    Hirano, M.2    Kobayashi, R.3    Hirano, T.4
  • 64
    • 0029025606 scopus 로고
    • The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis
    • Sudakin V., Ganoth D., Dahan A., Heller H., Hershko J., Luca F. C. et al. (1995) The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Biol. Cell 6: 185-197
    • (1995) Mol. Biol. Cell , vol.6 , pp. 185-197
    • Sudakin, V.1    Ganoth, D.2    Dahan, A.3    Heller, H.4    Hershko, J.5    Luca, F.C.6
  • 65
    • 0032529162 scopus 로고    scopus 로고
    • Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- Promoting complex at mitosis
    • Patra D. and Dunphy W. G. (1998) Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosis. Genes Dev. 12: 2549-2559
    • (1998) Genes Dev. , vol.12 , pp. 2549-2559
    • Patra, D.1    Dunphy, W.G.2
  • 66
    • 0032573374 scopus 로고    scopus 로고
    • Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex
    • Zachariae W., Schwab M., Nasmyth K. and Seufert W. (1998) Control of cyclin ubiquitination by CDK-regulated binding of Hct1 to the anaphase promoting complex. Science 282: 1721-1724
    • (1998) Science , vol.282 , pp. 1721-1724
    • Zachariae, W.1    Schwab, M.2    Nasmyth, K.3    Seufert, W.4
  • 67
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters J. M. (2002) The anaphase-promoting complex: proteolysis in mitosis and beyond. Mol. Cell 9: 931-943
    • (2002) Mol. Cell , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 68
    • 0023804548 scopus 로고
    • Polo, a mitotic mutant of Drosophila displaying abnormal spindle poles
    • Sunkel C. E. and Glover D. M. (1988) polo, a mitotic mutant of Drosophila displaying abnormal spindle poles. J. Cell Sci. 89 (Pt 1): 25-38
    • (1988) J. Cell Sci. , vol.89 , Issue.1 PART , pp. 25-38
    • Sunkel, C.E.1    Glover, D.M.2
  • 69
    • 0027173110 scopus 로고
    • A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5
    • Kitada K., Johnson A. L., Johnston L. H. and Sugino A. (1993) A multicopy suppressor gene of the Saccharomyces cerevisiae G1 cell cycle mutant gene dbf4 encodes a protein kinase and is identified as CDC5. Mol. Cell. Biol. 13: 4445-4457
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4445-4457
    • Kitada, K.1    Johnson, A.L.2    Johnston, L.H.3    Sugino, A.4
  • 70
    • 13244284602 scopus 로고    scopus 로고
    • Structure and function of Polo-like kinases
    • Lowery D. M., Lim D. and Yaffe M. B. (2005) Structure and function of Polo-like kinases. Oncogene 24: 248-259
    • (2005) Oncogene , vol.24 , pp. 248-259
    • Lowery, D.M.1    Lim, D.2    Yaffe, M.B.3
  • 71
    • 0242515843 scopus 로고    scopus 로고
    • Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates
    • Elia A. E., Cantley L. C. and Yaffe M. B. (2003) Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates. Science 299: 1228-1231
    • (2003) Science , vol.299 , pp. 1228-1231
    • Elia, A.E.1    Cantley, L.C.2    Yaffe, M.B.3
  • 72
    • 0031581099 scopus 로고    scopus 로고
    • On the regulation and function of human polo-like kinase 1 (PLK1): Effects of overexpression on cell cycle progression
    • Mundt K. E., Golsteyn R. M., Lane H. A. and Nigg E. A. (1997) On the regulation and function of human polo-like kinase 1 (PLK1): effects of overexpression on cell cycle progression. Biochem. Biophys. Res. Commun. 239: 377-385
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 377-385
    • Mundt, K.E.1    Golsteyn, R.M.2    Lane, H.A.3    Nigg, E.A.4
  • 73
    • 0037133203 scopus 로고    scopus 로고
    • Functional studies on the role of the C-terminal domain of mammalian polo-like kinase
    • USA
    • Jang Y. J., Lin C. Y., Ma S. and Erikson R. L. (2002) Functional studies on the role of the C-terminal domain of mammalian polo-like kinase. Proc. Natl. Acad. Sci. USA 99: 1984-1989
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 1984-1989
    • Jang, Y.J.1    Lin, C.Y.2    Ma, S.3    Erikson, R.L.4
  • 74
    • 0033986962 scopus 로고    scopus 로고
    • Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures
    • Song S., Grenfell T. Z., Garfield S., Erikson R. L. and Lee K. S. (2000) Essential function of the polo box of Cdc5 in subcellular localization and induction of cytokinetic structures. Mol. Cell. Biol. 20: 286-298
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 286-298
    • Song, S.1    Grenfell, T.Z.2    Garfield, S.3    Erikson, R.L.4    Lee, K.S.5
  • 75
    • 0032482986 scopus 로고    scopus 로고
    • Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk
    • USA
    • Lee K. S., Grenfell T. Z., Yarm F. R. and Erikson R. L. (1998) Mutation of the polo-box disrupts localization and mitotic functions of the mammalian polo kinase Plk. Proc. Natl. Acad. Sci. USA 95: 9301-9306
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 9301-9306
    • Lee, K.S.1    Grenfell, T.Z.2    Yarm, F.R.3    Erikson, R.L.4
  • 76
    • 0031785411 scopus 로고    scopus 로고
    • Cell cycle regulation of the Saccharomyces cerevisiae polo-like kinase cdc5p
    • Cheng L., Hunke L. and Hardy C. F. (1998) Cell cycle regulation of the Saccharomyces cerevisiae polo-like kinase cdc5p. Mol. Cell. Biol. 18: 7360-7370
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7360-7370
    • Cheng, L.1    Hunke, L.2    Hardy, C.F.3
  • 77
    • 0029079267 scopus 로고
    • Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function
    • Golsteyn R. M., Mundt K. E., Fry A. M. and Nigg E. A. (1995) Cell cycle regulation of the activity and subcellular localization of Plk1, a human protein kinase implicated in mitotic spindle function. J. Cell Biol. 129: 1617-1628
    • (1995) J. Cell Biol. , vol.129 , pp. 1617-1628
    • Golsteyn, R.M.1    Mundt, K.E.2    Fry, A.M.3    Nigg, E.A.4
  • 78
    • 0030924977 scopus 로고    scopus 로고
    • Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures
    • Lee K. S. and Erikson R. L. (1997) Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures. Mol. Cell. Biol. 17: 3408-3417
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3408-3417
    • Lee, K.S.1    Erikson, R.L.2
  • 79
    • 0033512308 scopus 로고    scopus 로고
    • Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1
    • Qian Y. W., Erikson E. and Maller J. L. (1999) Mitotic effects of a constitutively active mutant of the Xenopus polo-like kinase Plx1. Mol. Cell. Biol. 19: 8625-8632
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8625-8632
    • Qian, Y.W.1    Erikson, E.2    Maller, J.L.3
  • 80
    • 0037113919 scopus 로고    scopus 로고
    • Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase
    • Jang Y. J., Ma S., Terada Y. and Erikson R. L. (2002) Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase. J. Biol. Chem. 277: 44115-44120
    • (2002) J. Biol. Chem. , vol.277 , pp. 44115-44120
    • Jang, Y.J.1    Ma, S.2    Terada, Y.3    Erikson, R.L.4
  • 81
    • 0032573383 scopus 로고    scopus 로고
    • Purification and cloning of a protein kinase that phosphorylates and activates the polo-like kinase Plx1
    • Qian Y. W., Erikson E. and Maller J. L. (1998) Purification and cloning of a protein kinase that phosphorylates and activates the polo-like kinase Plx1. Science 282: 1701-1704
    • (1998) Science , vol.282 , pp. 1701-1704
    • Qian, Y.W.1    Erikson, E.2    Maller, J.L.3
  • 82
    • 3543011961 scopus 로고    scopus 로고
    • A feedback loop in the polo-like kinase activation pathway
    • Erikson E., Haystead T. A., Qian Y. W. and Maller J. L. (2004) A feedback loop in the polo-like kinase activation pathway. J. Biol. Chem. 279: 32219-32224
    • (2004) J. Biol. Chem. , vol.279 , pp. 32219-32224
    • Erikson, E.1    Haystead, T.A.2    Qian, Y.W.3    Maller, J.L.4
  • 83
    • 0037067758 scopus 로고    scopus 로고
    • Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1
    • Kelm O., Wind M., Lehmann W. D. and Nigg E. A. (2002) Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase Plx1. J. Biol. Chem. 277: 25247-25256
    • (2002) J. Biol. Chem. , vol.277 , pp. 25247-25256
    • Kelm, O.1    Wind, M.2    Lehmann, W.D.3    Nigg, E.A.4
  • 84
    • 0032473568 scopus 로고    scopus 로고
    • The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae
    • Shirayama M., Zachariae W., Ciosk R. and Nasmyth K. (1998) The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae. EMBO J. 17: 1336-1349
    • (1998) EMBO J. , vol.17 , pp. 1336-1349
    • Shirayama, M.1    Zachariae, W.2    Ciosk, R.3    Nasmyth, K.4
  • 85
    • 1642458099 scopus 로고    scopus 로고
    • Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells
    • Lindon C. and Pines J. (2004) Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells. J. Cell Biol. 164: 233-241
    • (2004) J. Cell Biol. , vol.164 , pp. 233-241
    • Lindon, C.1    Pines, J.2
  • 86
    • 2942615282 scopus 로고    scopus 로고
    • Polo-like kinases and the orchestration of cell division
    • Barr F. A., Sillje H. H. and Nigg E. A. (2004) Polo-like kinases and the orchestration of cell division. Nat. Rev. Mol. Cell. Biol. 5: 429-440
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 429-440
    • Barr, F.A.1    Sillje, H.H.2    Nigg, E.A.3
  • 87
    • 18344366048 scopus 로고    scopus 로고
    • Getting in and out of mitosis with Polo-like kinase-1
    • van Vugt M. A. and Medema R. H. (2005) Getting in and out of mitosis with Polo-like kinase-1. Oncogene 24: 2844-2859
    • (2005) Oncogene , vol.24 , pp. 2844-2859
    • Van Vugt, M.A.1    Medema, R.H.2
  • 88
    • 0035906861 scopus 로고    scopus 로고
    • Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast
    • Alexandra G., Uhlmann F., Mechtler K., Poupart M. A. and Nasmyth K. (2001) Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast. Cell 105: 459-472
    • (2001) Cell , vol.105 , pp. 459-472
    • Alexandra, G.1    Uhlmann, F.2    Mechtler, K.3    Poupart, M.A.4    Nasmyth, K.5
  • 89
    • 0036334279 scopus 로고    scopus 로고
    • Plk phosphorylation regulates the microtubule-stabilizing protein TCTP
    • Yarm F. R. (2002) Plk phosphorylation regulates the microtubule- stabilizing protein TCTP. Mol. Cell. Biol. 22: 6209-6221
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6209-6221
    • Yarm, F.R.1
  • 90
    • 0037672151 scopus 로고    scopus 로고
    • Polo-like kinase 1 regulates N1p, a centrosome protein involved in microtubule nucleation
    • Casenghi M., Meraldi P., Weinhart U., Duncan P. I., Korner R. and Nigg E. A. (2003) Polo-like kinase 1 regulates N1p, a centrosome protein involved in microtubule nucleation. Dev. Cell 5: 113-125
    • (2003) Dev. Cell , vol.5 , pp. 113-125
    • Casenghi, M.1    Meraldi, P.2    Weinhart, U.3    Duncan, P.I.4    Korner, R.5    Nigg, E.A.6
  • 91
    • 0038686507 scopus 로고    scopus 로고
    • A role for Plk1 phosphorylation of NudC in cytokinesis
    • Zhou T., Aumais J. P., Liu X., Yu-Lee L. Y. and Erikson R. L. (2003) A role for Plk1 phosphorylation of NudC in cytokinesis. Dev. Cell 5: 127-138
    • (2003) Dev. Cell , vol.5 , pp. 127-138
    • Zhou, T.1    Aumais, J.P.2    Liu, X.3    Yu-Lee, L.Y.4    Erikson, R.L.5
  • 92
    • 0031991880 scopus 로고    scopus 로고
    • PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression
    • Kotani S., Tugendreich S., Fujii M., Jorgensen P. M., Watanabe N., Hoog C. et al. (1998) PKA and MPF-activated polo-like kinase regulate anaphase-promoting complex activity and mitosis progression. Mol. Cell 1: 371-380
    • (1998) Mol. Cell , vol.1 , pp. 371-380
    • Kotani, S.1    Tugendreich, S.2    Fujii, M.3    Jorgensen, P.M.4    Watanabe, N.5    Hoog, C.6
  • 93
    • 0346363801 scopus 로고    scopus 로고
    • Mitotic regulation of the human anaphase-promoting complex by phosphorylation
    • Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J. et al. (2003) Mitotic regulation of the human anaphase-promoting complex by phosphorylation. EMBO J. 22: 6598-6609
    • (2003) EMBO J. , vol.22 , pp. 6598-6609
    • Kraft, C.1    Herzog, F.2    Gieffers, C.3    Mechtler, K.4    Hagting, A.5    Pines, J.6
  • 94
    • 2542459341 scopus 로고    scopus 로고
    • Adaptation of a DNA replication checkpoint response depends upon inactivation of Claspin by the Polo-like kinase
    • Yoo H. Y., Kumagai A., Shevchenko A., Shevchenko A. and Dunphy W. G. (2004) Adaptation of a DNA replication checkpoint response depends upon inactivation of Claspin by the Polo-like kinase. Cell 117: 575-588
    • (2004) Cell , vol.117 , pp. 575-588
    • Yoo, H.Y.1    Kumagai, A.2    Shevchenko, A.3    Shevchenko, A.4    Dunphy, W.G.5
  • 95
    • 0344413633 scopus 로고    scopus 로고
    • G2 and spindle assembly checkpoint adaptation, and tetraploidy arrest: Implications for intrinsic and chemically induced genomic instability
    • Andreassen P. R., Lohez O. D. and Margolis R. L. (2003) G2 and spindle assembly checkpoint adaptation, and tetraploidy arrest: implications for intrinsic and chemically induced genomic instability. Mutat. Res. 532: 245-253
    • (2003) Mutat. Res. , vol.532 , pp. 245-253
    • Andreassen, P.R.1    Lohez, O.D.2    Margolis, R.L.3
  • 96
    • 0030885666 scopus 로고    scopus 로고
    • CDC5 and CKII control adaptation to the yeast DNA damage checkpoint
    • Toczyski D. P., Galgoczy D. J. and Hartwell L. H. (1997) CDC5 and CKII control adaptation to the yeast DNA damage checkpoint. Cell 90: 1097-1106
    • (1997) Cell , vol.90 , pp. 1097-1106
    • Toczyski, D.P.1    Galgoczy, D.J.2    Hartwell, L.H.3
  • 98
    • 3543146736 scopus 로고    scopus 로고
    • Polo-like kinase 1 inactivation following mitotic DNA damaging treatments is independent of ataxia telangiectasia mutated kinase
    • Yuan J. H., Feng Y., Fisher R. H., Maloid S., Longo D. L. and Ferris D. K. (2004) Polo-like kinase 1 inactivation following mitotic DNA damaging treatments is independent of ataxia telangiectasia mutated kinase. Mol. Cancer Res. 2: 417-426
    • (2004) Mol. Cancer Res. , vol.2 , pp. 417-426
    • Yuan, J.H.1    Feng, Y.2    Fisher, R.H.3    Maloid, S.4    Longo, D.L.5    Ferris, D.K.6
  • 99
    • 0035834727 scopus 로고    scopus 로고
    • Inhibition of Polo-like kinase-1 by DNA damage occurs in an ATM- Or ATR-dependent fashion
    • van Vugt M. A., Smits V. A., Klompmaker R. and Medema R. H. (2001) Inhibition of Polo-like kinase-1 by DNA damage occurs in an ATM- or ATR-dependent fashion. J. Biol. Chem. 276: 41656-41660
    • (2001) J. Biol. Chem. , vol.276 , pp. 41656-41660
    • Van Vugt, M.A.1    Smits, V.A.2    Klompmaker, R.3    Medema, R.H.4
  • 101
    • 4444321565 scopus 로고    scopus 로고
    • Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells
    • van Vugt M. A., Bras A. and Medema R. H. (2004) Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol. Cell 15: 799-811
    • (2004) Mol. Cell , vol.15 , pp. 799-811
    • Van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 102
    • 0038492408 scopus 로고    scopus 로고
    • Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate
    • Nakajima H., Toyoshima-Morimoto F., Taniguchi E. and Nishida E. (2003) Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate. J. Biol. Chem. 278: 25277-25280
    • (2003) J. Biol. Chem. , vol.278 , pp. 25277-25280
    • Nakajima, H.1    Toyoshima-Morimoto, F.2    Taniguchi, E.3    Nishida, E.4
  • 103
  • 104
    • 0024294395 scopus 로고
    • Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase
    • Osmani S. A., Pu R. T. and Morris N. R. (1988) Mitotic induction and maintenance by overexpression of a G2-specific gene that encodes a potential protein kinase. Cell 53: 237-244
    • (1988) Cell , vol.53 , pp. 237-244
    • Osmani, S.A.1    Pu, R.T.2    Morris, N.R.3
  • 105
    • 0037048312 scopus 로고    scopus 로고
    • The Nek2 protein kinase: A novel regulator of centrosome structure
    • Fry A. M. (2002) The Nek2 protein kinase: a novel regulator of centrosome structure. Oncogene 21: 6184-6194
    • (2002) Oncogene , vol.21 , pp. 6184-6194
    • Fry, A.M.1
  • 106
    • 0033523093 scopus 로고    scopus 로고
    • Activity of the human centrosomal kinase, Nek2, depends on an unusual leucine zipper dimerization motif
    • Fry A. M., Arnaud L. and Nigg E. A. (1999) Activity of the human centrosomal kinase, Nek2, depends on an unusual leucine zipper dimerization motif. J. Biol. Chem. 274: 16304-16310
    • (1999) J. Biol. Chem. , vol.274 , pp. 16304-16310
    • Fry, A.M.1    Arnaud, L.2    Nigg, E.A.3
  • 107
    • 0036336894 scopus 로고    scopus 로고
    • The MAPK pathway triggers activation of Nek2 during chromosome condensation in mouse spermatocytes
    • Di Agostino S., Rossi P., Geremia R. and Sette C. (2002) The MAPK pathway triggers activation of Nek2 during chromosome condensation in mouse spermatocytes. Development 129: 1715-1727
    • (2002) Development , vol.129 , pp. 1715-1727
    • Di Agostino, S.1    Rossi, P.2    Geremia, R.3    Sette, C.4
  • 108
    • 0034661499 scopus 로고    scopus 로고
    • NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1
    • Helps N. R., Luo X., Barker H. M. and Cohen P. T. (2000) NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1. Biochem. J. 349: 509-518
    • (2000) Biochem. J. , vol.349 , pp. 509-518
    • Helps, N.R.1    Luo, X.2    Barker, H.M.3    Cohen, P.T.4
  • 109
    • 0029011885 scopus 로고
    • Substrate specificity and cell cycle regulation of the Nek2 protein kinase, a potential human homolog of the mitotic regulator NIMA of Aspergillus nidulans
    • Fry A. M., Schultz S. J., Bartek J. and Nigg E. A. (1995) Substrate specificity and cell cycle regulation of the Nek2 protein kinase, a potential human homolog of the mitotic regulator NIMA of Aspergillus nidulans. J. Biol. Chem. 270: 12899-12905
    • (1995) J. Biol. Chem. , vol.270 , pp. 12899-12905
    • Fry, A.M.1    Schultz, S.J.2    Bartek, J.3    Nigg, E.A.4
  • 110
    • 0037126610 scopus 로고    scopus 로고
    • APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box
    • Hames R. S., Wattam S. L., Yamano H., Bacchieri R. and Fry A. M. (2001) APC/C-mediated destruction of the centrosomal kinase Nek2A occurs in early mitosis and depends upon a cyclin A-type D-box. EMBO J. 20: 7117-7127
    • (2001) EMBO J. , vol.20 , pp. 7117-7127
    • Hames, R.S.1    Wattam, S.L.2    Yamano, H.3    Bacchieri, R.4    Fry, A.M.5
  • 111
    • 0032518798 scopus 로고    scopus 로고
    • A centrosomal function for the human Nek2 protein kinase, a member of the NIMA family of cell cycle regulators
    • Fry A. M., Meraldi P. and Nigg E. A. (1998) A centrosomal function for the human Nek2 protein kinase, a member of the NIMA family of cell cycle regulators. EMBO J. 17: 470-481
    • (1998) EMBO J. , vol.17 , pp. 470-481
    • Fry, A.M.1    Meraldi, P.2    Nigg, E.A.3
  • 112
    • 0034753402 scopus 로고    scopus 로고
    • Centrosome cohesion is regulated by a balance of kinase and phosphatase activities
    • Meraldi P. and Nigg E. A. (2001) Centrosome cohesion is regulated by a balance of kinase and phosphatase activities. J. Cell Sci. 114: 3749-3757
    • (2001) J. Cell Sci. , vol.114 , pp. 3749-3757
    • Meraldi, P.1    Nigg, E.A.2
  • 113
    • 0032578008 scopus 로고    scopus 로고
    • C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2
    • Fry A. M., Mayor T., Meraldi P., Stierhof Y. D., Tanaka K. and Nigg E. A. (1998) C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2. J. Cell Biol. 141: 1563-1574
    • (1998) J. Cell Biol. , vol.141 , pp. 1563-1574
    • Fry, A.M.1    Mayor, T.2    Meraldi, P.3    Stierhof, Y.D.4    Tanaka, K.5    Nigg, E.A.6
  • 114
    • 0034645037 scopus 로고    scopus 로고
    • The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion
    • Mayor T., Stierhof Y. D., Tanaka K., Fry A. M. and Nigg E. A. (2000) The centrosomal protein C-Nap1 is required for cell cycle-regulated centrosome cohesion. J. Cell Biol. 151: 837-846
    • (2000) J. Cell Biol. , vol.151 , pp. 837-846
    • Mayor, T.1    Stierhof, Y.D.2    Tanaka, K.3    Fry, A.M.4    Nigg, E.A.5
  • 115
    • 4143051237 scopus 로고    scopus 로고
    • Inhibition of centrosome separation after DNA damage: A role for Nek2
    • Fletcher L., Cerniglia G. J., Nigg E. A., Yend T. J. and Muschel R. J. (2004) Inhibition of centrosome separation after DNA damage: a role for Nek2. Radiat Res 162: 128-135
    • (2004) Radiat Res , vol.162 , pp. 128-135
    • Fletcher, L.1    Cerniglia, G.J.2    Nigg, E.A.3    Yend, T.J.4    Muschel, R.J.5
  • 116
    • 0035813136 scopus 로고    scopus 로고
    • The G(2) DNA damage checkpoint delays expression of genes encoding mitotic regulators
    • Crawford D. F. and Piwnica-Worms H. (2001) The G(2) DNA damage checkpoint delays expression of genes encoding mitotic regulators. J. Biol. Chem. 276: 37166-37177
    • (2001) J. Biol. Chem. , vol.276 , pp. 37166-37177
    • Crawford, D.F.1    Piwnica-Worms, H.2
  • 117
    • 0033226802 scopus 로고    scopus 로고
    • Aurora/Ipl1p-related kinases, a new oncogenic family of mitotic serine-threonine kinases
    • Giet R. and Prigent C. (1999) Aurora/Ipl1p-related kinases, a new oncogenic family of mitotic serine-threonine kinases. J. Cell Sci. 112 (Pt 21): 3591-3601
    • (1999) J. Cell Sci. , vol.112 , Issue.21 PART , pp. 3591-3601
    • Giet, R.1    Prigent, C.2
  • 118
    • 0027515186 scopus 로고
    • Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast
    • Chan C. S. and Botstein D. (1993) Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics 135: 677-691
    • (1993) Genetics , vol.135 , pp. 677-691
    • Chan, C.S.1    Botstein, D.2
  • 119
    • 0028938482 scopus 로고
    • Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles
    • Glover D. M., Leibowitz M. H., McLean D. A. and Parry H. (1995) Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles. Cell 81: 95-105
    • (1995) Cell , vol.81 , pp. 95-105
    • Glover, D.M.1    Leibowitz, M.H.2    McLean, D.A.3    Parry, H.4
  • 120
    • 0033106222 scopus 로고    scopus 로고
    • The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast
    • Biggins S., Severin F. F., Bhalla N., Sassoon I., Hyman A. A. and Murray A. W. (1999) The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast. Genes Dev. 13: 532-544
    • (1999) Genes Dev. , vol.13 , pp. 532-544
    • Biggins, S.1    Severin, F.F.2    Bhalla, N.3    Sassoon, I.4    Hyman, A.A.5    Murray, A.W.6
  • 121
    • 0032489332 scopus 로고    scopus 로고
    • cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2
    • Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D. J. et al. (1998) cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2. Biochem. Biophys. Res. Commun. 244: 285-292
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 285-292
    • Shindo, M.1    Nakano, H.2    Kuroyanagi, H.3    Shirasawa, T.4    Mihara, M.5    Gilbert, D.J.6
  • 122
    • 0032100685 scopus 로고    scopus 로고
    • A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers
    • Bischoff J. R., Anderson L., Zhu Y., Mossie K., Ng L., Souza B. et al. (1998) A homologue of Drosophila aurora kinase is oncogenic and amplified in human colorectal cancers. EMBO J. 17: 3052-3065
    • (1998) EMBO J. , vol.17 , pp. 3052-3065
    • Bischoff, J.R.1    Anderson, L.2    Zhu, Y.3    Mossie, K.4    Ng, L.5    Souza, B.6
  • 123
    • 0038323936 scopus 로고    scopus 로고
    • Dynamic association of a tumor amplified kinase, Aurora-A, with the centrosome and mitotic spindle
    • Stenoien D. L., Sen S., Mancini M. A. and Brinkley B. R. (2003) Dynamic association of a tumor amplified kinase, Aurora-A, with the centrosome and mitotic spindle. Cell Motil. Cytoskeleton 55: 134-146
    • (2003) Cell Motil. Cytoskeleton , vol.55 , pp. 134-146
    • Stenoien, D.L.1    Sen, S.2    Mancini, M.A.3    Brinkley, B.R.4
  • 125
    • 0141429171 scopus 로고    scopus 로고
    • Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
    • Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M. et al. (2003) Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Cell 114: 585-598
    • (2003) Cell , vol.114 , pp. 585-598
    • Hirota, T.1    Kunitoku, N.2    Sasayama, T.3    Marumoto, T.4    Zhang, D.5    Nitta, M.6
  • 126
    • 0030962953 scopus 로고    scopus 로고
    • A putative serine/threonine kinase encoding gene BTAK on chromosome 20q13 is amplified and overexpressed in human breast cancer cell lines
    • Sen S., Zhou H. and White R. A. (1997) A putative serine/threonine kinase encoding gene BTAK on chromosome 20q13 is amplified and overexpressed in human breast cancer cell lines. Oncogene 14: 2195-2200
    • (1997) Oncogene , vol.14 , pp. 2195-2200
    • Sen, S.1    Zhou, H.2    White, R.A.3
  • 127
    • 0031714080 scopus 로고    scopus 로고
    • Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation
    • Zhou H., Kuang J., Zhong L., Kuo W. L., Gray J. W., Sahin A. et al. (1998) Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation. Nat. Genet. 20: 189-193
    • (1998) Nat. Genet. , vol.20 , pp. 189-193
    • Zhou, H.1    Kuang, J.2    Zhong, L.3    Kuo, W.L.4    Gray, J.W.5    Sahin, A.6
  • 130
    • 0036714512 scopus 로고    scopus 로고
    • Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit
    • Littlepage L. E. and Ruderman J. V. (2002) Identification of a new APC/C recognition domain, the A box, which is required for the Cdh1-dependent destruction of the kinase Aurora-A during mitotic exit. Genes Dev. 16: 2274-2285
    • (2002) Genes Dev. , vol.16 , pp. 2274-2285
    • Littlepage, L.E.1    Ruderman, J.V.2
  • 131
    • 12244301635 scopus 로고    scopus 로고
    • The D-Box-activating domain (DAD) is a new proteolysis signal that stimulates the silent D-Box sequence of Aurora-A
    • Castro A., Vigneron S., Bernis C., Labbe J. C., Prigent C. and Lorca T. (2002) The D-Box-activating domain (DAD) is a new proteolysis signal that stimulates the silent D-Box sequence of Aurora-A. EMBO Rep. 3: 1209-1214
    • (2002) EMBO Rep. , vol.3 , pp. 1209-1214
    • Castro, A.1    Vigneron, S.2    Bernis, C.3    Labbe, J.C.4    Prigent, C.5    Lorca, T.6
  • 133
    • 0034609753 scopus 로고    scopus 로고
    • The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation
    • Walter A. O., Seghezzi W., Korver W., Sheung J. and Lees E. (2000) The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation. Oncogene 19: 4906-4916
    • (2000) Oncogene , vol.19 , pp. 4906-4916
    • Walter, A.O.1    Seghezzi, W.2    Korver, W.3    Sheung, J.4    Lees, E.5
  • 135
    • 0029964613 scopus 로고    scopus 로고
    • Requirement for cAMP-PKA pathway activation by M phase-promoting factor in the transition from mitosis to interphase
    • Grieco D., Porcellini A., Avvedimento E. V. and Gottesman M. E. (1996) Requirement for cAMP-PKA pathway activation by M phase-promoting factor in the transition from mitosis to interphase. Science 271: 1718-1723
    • (1996) Science , vol.271 , pp. 1718-1723
    • Grieco, D.1    Porcellini, A.2    Avvedimento, E.V.3    Gottesman, M.E.4
  • 136
    • 0842299091 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
    • Haydon C. E., Eyers P. A., Aveline-Wolf L. D., Resing K. A., Maller J. L. and Ahn N. G. (2003) Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography. Mol. Cell. Proteomics 2: 1055-1067
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1055-1067
    • Haydon, C.E.1    Eyers, P.A.2    Aveline-Wolf, L.D.3    Resing, K.A.4    Maller, J.L.5    Ahn, N.G.6
  • 137
    • 0036142218 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3: Spatiotemporal regulation by mammalian Aurora kinases
    • Crosio C., Fimia G. M., Loury R., Kimura M., Okano Y., Zhou H. et al. (2002) Mitotic phosphorylation of histone H3: spatiotemporal regulation by mammalian Aurora kinases. Mol. Cell. Biol. 22: 874-885
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 874-885
    • Crosio, C.1    Fimia, G.M.2    Loury, R.3    Kimura, M.4    Okano, Y.5    Zhou, H.6
  • 138
    • 26944442735 scopus 로고    scopus 로고
    • The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A
    • Zhao Z. S., Lim J. P., Ng Y. W., Lim L. and Manser E. (2005) The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A. Mol. Cell 20: 237-249
    • (2005) Mol. Cell , vol.20 , pp. 237-249
    • Zhao, Z.S.1    Lim, J.P.2    Ng, Y.W.3    Lim, L.4    Manser, E.5
  • 139
    • 0037446847 scopus 로고    scopus 로고
    • A novel mechanism for activation of the protein kinase aurora a
    • Eyers P. A., Erikson E., Chen L. G. and Maller J. L. (2003) A novel mechanism for activation of the protein kinase aurora a. Curr. Biol. 13: 691-697
    • (2003) Curr. Biol. , vol.13 , pp. 691-697
    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
  • 141
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • Bayliss R., Sardon T., Vernos I. and Conti E. (2003) Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell 12: 851-862
    • (2003) Mol. Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 142
    • 0035824660 scopus 로고    scopus 로고
    • Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle
    • Katayama H., Zhou H., Li Q., Tatsuka M. and Sen S. (2001) Interaction and feedback regulation between STK15/BTAK/Aurora-A kinase and protein phosphatase 1 through mitotic cell division cycle. J. Biol. Chem. 276: 46219-46224
    • (2001) J. Biol. Chem. , vol.276 , pp. 46219-46224
    • Katayama, H.1    Zhou, H.2    Li, Q.3    Tatsuka, M.4    Sen, S.5
  • 143
    • 2942590333 scopus 로고    scopus 로고
    • Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein
    • USA
    • Satinover D. L., Leach C. A., Stukenberg P. T. and Brautigan D. L. (2004) Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein. Proc. Natl. Acad. Sci. USA 101: 8625-8630
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 8625-8630
    • Satinover, D.L.1    Leach, C.A.2    Stukenberg, P.T.3    Brautigan, D.L.4
  • 144
    • 0037160088 scopus 로고    scopus 로고
    • Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase
    • Kiat L. S., Hui K. M. and Gopalan G. (2002) Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase. J. Biol. Chem. 277: 45558-45565
    • (2002) J. Biol. Chem. , vol.277 , pp. 45558-45565
    • Kiat, L.S.1    Hui, K.M.2    Gopalan, G.3
  • 145
    • 3042734502 scopus 로고    scopus 로고
    • Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2-M transition
    • Dutertre S., Cazales M., Quaranta M., Froment C., Trabut V., Dozier C. et al. (2004) Phosphorylation of CDC25B by Aurora-A at the centrosome contributes to the G2-M transition. J. Cell Sci. 117: 2523-2531
    • (2004) J. Cell Sci. , vol.117 , pp. 2523-2531
    • Dutertre, S.1    Cazales, M.2    Quaranta, M.3    Froment, C.4    Trabut, V.5    Dozier, C.6
  • 147
    • 10644227569 scopus 로고    scopus 로고
    • Aurora-A abrogation of p53 DNA binding and transactivation activity by phosphorylation of serine 215
    • Liu Q., Kaneko S., Yang L., Feldman R. I., Nicosia S. V., Chen J. et al. (2004) Aurora-A abrogation of p53 DNA binding and transactivation activity by phosphorylation of serine 215. J. Biol. Chem. 279: 52175-52182
    • (2004) J. Biol. Chem. , vol.279 , pp. 52175-52182
    • Liu, Q.1    Kaneko, S.2    Yang, L.3    Feldman, R.I.4    Nicosia, S.V.5    Chen, J.6
  • 148
    • 18644380150 scopus 로고    scopus 로고
    • Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells
    • Marumoto T., Hirota T., Morisaki T., Kunitoku N., Zhang D., Ichikawa Y. et al. (2002) Roles of aurora-A kinase in mitotic entry and G2 checkpoint in mammalian cells. Genes Cells. 7: 1173-1182
    • (2002) Genes Cells. , vol.7 , pp. 1173-1182
    • Marumoto, T.1    Hirota, T.2    Morisaki, T.3    Kunitoku, N.4    Zhang, D.5    Ichikawa, Y.6
  • 149
    • 0033231927 scopus 로고    scopus 로고
    • The Aurora/Ipl1p kinase family: Regulators of chromosome segregation and cytokinesis
    • Bischoff J. R. and Plowman G. D. (1999) The Aurora/Ipl1p kinase family: regulators of chromosome segregation and cytokinesis. Trends Cell Biol. 9: 454-459
    • (1999) Trends Cell Biol. , vol.9 , pp. 454-459
    • Bischoff, J.R.1    Plowman, G.D.2
  • 150
    • 11144354860 scopus 로고    scopus 로고
    • Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis
    • Yasui Y., Urano T., Kawajiri A., Nagata K., Tatsuka M., Saya H. et al. (2004) Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. J. Biol. Chem. 279: 12997-13003
    • (2004) J. Biol. Chem. , vol.279 , pp. 12997-13003
    • Yasui, Y.1    Urano, T.2    Kawajiri, A.3    Nagata, K.4    Tatsuka, M.5    Saya, H.6
  • 151
    • 0034618724 scopus 로고    scopus 로고
    • INCENP binds the Aurora-related kinase AIRK2 and is required to target it to chromosomes, the central spindle and cleavage furrow
    • Adams R. R., Wheatley S. P., Gouldsworthy A. M., Kandels-Lewis S. E., Carmena M., Smythe C. et al. (2000) INCENP binds the Aurora-related kinase AIRK2 and is required to target it to chromosomes, the central spindle and cleavage furrow. Curr. Biol. 10: 1075-1078
    • (2000) Curr. Biol. , vol.10 , pp. 1075-1078
    • Adams, R.R.1    Wheatley, S.P.2    Gouldsworthy, A.M.3    Kandels-Lewis, S.E.4    Carmena, M.5    Smythe, C.6
  • 152
    • 0037008684 scopus 로고    scopus 로고
    • Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B Kinase stimulates Aurora B kinase activity
    • Bishop J. D. and Schumacher J. M. (2002) Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B Kinase stimulates Aurora B kinase activity. J. Biol. Chem. 277: 27577-27580
    • (2002) J. Biol. Chem. , vol.277 , pp. 27577-27580
    • Bishop, J.D.1    Schumacher, J.M.2
  • 153
    • 0032472915 scopus 로고    scopus 로고
    • AIM-1: A mammalian midbody-associated protein required for cytokinesis
    • Terada Y., Tatsuka M., Suzuki F., Yasuda Y., Fujita S. and Otsu M. (1998) AIM-1: a mammalian midbody-associated protein required for cytokinesis. EMBO J. 17: 667-676
    • (1998) EMBO J. , vol.17 , pp. 667-676
    • Terada, Y.1    Tatsuka, M.2    Suzuki, F.3    Yasuda, Y.4    Fujita, S.5    Otsu, M.6
  • 154
    • 0035911159 scopus 로고    scopus 로고
    • Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis
    • Giet R. and Glover D. M. (2001) Drosophila aurora B kinase is required for histone H3 phosphorylation and condensin recruitment during chromosome condensation and to organize the central spindle during cytokinesis. J. Cell Biol. 152: 669-682
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 155
    • 0034604354 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
    • Hsu J. Y., Sun Z. W., Li X., Reuben M., Tatchell K., Bishop D. K. et al. (2000) Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell 102: 279-291
    • (2000) Cell , vol.102 , pp. 279-291
    • Hsu, J.Y.1    Sun, Z.W.2    Li, X.3    Reuben, M.4    Tatchell, K.5    Bishop, D.K.6
  • 156
    • 0036158780 scopus 로고    scopus 로고
    • Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation
    • Goto H., Yasui Y., Nigg E. A. and Inagaki M. (2002) Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. Genes Cells 7: 11-17
    • (2002) Genes Cells , vol.7 , pp. 11-17
    • Goto, H.1    Yasui, Y.2    Nigg, E.A.3    Inagaki, M.4
  • 157
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel M. J., Wei Y., Mancini M. A., Van Hooser A., Ranalli T., Brinkley B. R. et al. (1997) Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106: 348-360
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1    Wei, Y.2    Mancini, M.A.3    Van Hooser, A.4    Ranalli, T.5    Brinkley, B.R.6
  • 158
    • 0032442522 scopus 로고    scopus 로고
    • Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation
    • Van Hooser A., Goodrich D. W., Allis C. D., Brinkley B. R. and Mancini M. A. (1998) Histone H3 phosphorylation is required for the initiation, but not maintenance, of mammalian chromosome condensation. J. Cell Sci. 111 (Pt 23): 3497-3506
    • (1998) J. Cell Sci. , vol.111 , Issue.23 PART , pp. 3497-3506
    • Van Hooser, A.1    Goodrich, D.W.2    Allis, C.D.3    Brinkley, B.R.4    Mancini, M.A.5
  • 159
    • 28844477653 scopus 로고    scopus 로고
    • Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation
    • doi: 10.1038/nature04219
    • Fischle W., Tseng B. S., Dormann H. L., Ueberheide B. M., Garcia B. A., Shabanowitz J. et al. (2005) Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation. Nature doi: 10.1038/nature04219
    • (2005) Nature
    • Fischle, W.1    Tseng, B.S.2    Dormann, H.L.3    Ueberheide, B.M.4    Garcia, B.A.5    Shabanowitz, J.6
  • 160
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • doi: 10.1038/nature04254
    • Hirota T., Lipp J. J., Toh B. H. and Peters J. M. (2005) Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature doi: 10.1038/nature04254
    • (2005) Nature
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 161
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • Ditchfield C., Johnson V. L., Tighe A., Ellston R., Haworth C., Johnson T. et al. (2003) Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. J. Cell Biol. 161: 267-280
    • (2003) J. Cell Biol. , vol.161 , pp. 267-280
    • Ditchfield, C.1    Johnson, V.L.2    Tighe, A.3    Ellston, R.4    Haworth, C.5    Johnson, T.6
  • 162
    • 0038746733 scopus 로고    scopus 로고
    • The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint
    • Hauf S., Cole R. W., LaTerra S., Zimmer C., Schnapp G., Walter R. et al. (2003) The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J. Cell Biol. 161: 281-294
    • (2003) J. Cell Biol. , vol.161 , pp. 281-294
    • Hauf, S.1    Cole, R.W.2    LaTerra, S.3    Zimmer, C.4    Schnapp, G.5    Walter, R.6
  • 164
    • 1542290607 scopus 로고    scopus 로고
    • Aurora B phosphorylates centromeric MCAK and regulates its localization and microtubule depolymerization activity
    • Lan W., Zhang X., Kline-Smith S. L., Rosasco S. E., Barrett-Wilt G. A., Shabanowitz J. et al. (2004) Aurora B phosphorylates centromeric MCAK and regulates its localization and microtubule depolymerization activity. Curr. Biol. 14: 273-286
    • (2004) Curr. Biol. , vol.14 , pp. 273-286
    • Lan, W.1    Zhang, X.2    Kline-Smith, S.L.3    Rosasco, S.E.4    Barrett-Wilt, G.A.5    Shabanowitz, J.6
  • 165
    • 2542495883 scopus 로고    scopus 로고
    • Differentiation of cytoplasmic and meiotic spindle assembly MCAK functions by Aurora B-dependent phosphorylation
    • Ohi R., Sapra T., Howard J. and Mitchison T. J. (2004) Differentiation of cytoplasmic and meiotic spindle assembly MCAK functions by Aurora B-dependent phosphorylation. Mol. Biol. Cell 15: 2895-2906
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2895-2906
    • Ohi, R.1    Sapra, T.2    Howard, J.3    Mitchison, T.J.4
  • 166
    • 0037424487 scopus 로고    scopus 로고
    • Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process
    • Goto H., Yasui Y., Kawajiri A., Nigg E. A., Terada Y., Tatsuka M. et al. (2003) Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J. Biol. Chem. 278: 8526-8530
    • (2003) J. Biol. Chem. , vol.278 , pp. 8526-8530
    • Goto, H.1    Yasui, Y.2    Kawajiri, A.3    Nigg, E.A.4    Terada, Y.5    Tatsuka, M.6
  • 167
    • 0017171619 scopus 로고
    • Adenosine 3′:5′-monophosphate content and actions in the division cycle of synchronized HeLa cells
    • Zeilig C. E., Johnson R. A., Sutherland E. W. and Friedman D. L. (1976) Adenosine 3′:5′-monophosphate content and actions in the division cycle of synchronized HeLa cells. J. Cell Biol. 71: 515-534
    • (1976) J. Cell Biol. , vol.71 , pp. 515-534
    • Zeilig, C.E.1    Johnson, R.A.2    Sutherland, E.W.3    Friedman, D.L.4
  • 168
    • 0025034980 scopus 로고
    • Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae
    • Smith M. E., Dickinson J. R. and Wheals A. E. (1990) Intracellular and extracellular levels of cyclic AMP during the cell cycle of Saccharomyces cerevisiae. Yeast 6: 53-60
    • (1990) Yeast , vol.6 , pp. 53-60
    • Smith, M.E.1    Dickinson, J.R.2    Wheals, A.E.3
  • 169
    • 0028138344 scopus 로고
    • A role for cAMP-dependent protein kinase in early embryonic divisions
    • USA
    • Grieco D., Avvedimento E. V. and Gottesman M. E. (1994) A role for cAMP-dependent protein kinase in early embryonic divisions. Proc. Natl. Acad. Sci. USA 91: 9896-9900
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 9896-9900
    • Grieco, D.1    Avvedimento, E.V.2    Gottesman, M.E.3
  • 170
    • 0029857172 scopus 로고    scopus 로고
    • 20S cyclosome complex formation and proteolytic activity inhibited by the cAMP/PKA pathway
    • Yamashita Y. M., Nakaseko Y., Samejima I., Kumada K., Yamada H., Michaelson D. et al. (1996) 20S cyclosome complex formation and proteolytic activity inhibited by the cAMP/PKA pathway. Nature 384: 276-279
    • (1996) Nature , vol.384 , pp. 276-279
    • Yamashita, Y.M.1    Nakaseko, Y.2    Samejima, I.3    Kumada, K.4    Yamada, H.5    Michaelson, D.6
  • 171
    • 0029826437 scopus 로고    scopus 로고
    • Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+
    • Ishii K., Kumada K., Toda T. and Yanagida M. (1996) Requirement for PP1 phosphatase and 20S cyclosome/APC for the onset of anaphase is lessened by the dosage increase of a novel gene sds23+. EMBO J. 15: 6629-6640
    • (1996) EMBO J. , vol.15 , pp. 6629-6640
    • Ishii, K.1    Kumada, K.2    Toda, T.3    Yanagida, M.4
  • 172
    • 0032807749 scopus 로고    scopus 로고
    • Protein kinase A-dependent and -independent signaling pathways contribute to cyclic AMP-stimulated proliferation
    • Cass L. A., Summers S. A., Prendergast G. V., Backer J. M., Birnbaum M. J. and Meinkoth J. L. (1999) Protein kinase A-dependent and -independent signaling pathways contribute to cyclic AMP-stimulated proliferation. Mol. Cell. Biol. 19: 5882-5891
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5882-5891
    • Cass, L.A.1    Summers, S.A.2    Prendergast, G.V.3    Backer, J.M.4    Birnbaum, M.J.5    Meinkoth, J.L.6
  • 173
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna L. A. and Ruzzene M. (1996) How do protein kinases recognize their substrates? Biochim. Biophys. Acta 1314: 191-225
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 174
    • 0025300349 scopus 로고
    • A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle
    • Levin D. E., Fields F. O., Kunisawa R., Bishop J. M. and Thorner J. (1990) A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle. Cell 62: 213-224
    • (1990) Cell , vol.62 , pp. 213-224
    • Levin, D.E.1    Fields, F.O.2    Kunisawa, R.3    Bishop, J.M.4    Thorner, J.5
  • 175
    • 0030722721 scopus 로고    scopus 로고
    • A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition
    • Sun B., Murray N. R. and Fields A. P. (1997) A role for nuclear phosphatidylinositol-specific phospholipase C in the G2/M phase transition. J. Biol. Chem. 272: 26313-26317
    • (1997) J. Biol. Chem. , vol.272 , pp. 26313-26317
    • Sun, B.1    Murray, N.R.2    Fields, A.P.3
  • 176
    • 0029871758 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes
    • Takai Y., Ogawara M., Tomono Y., Moritoh C., Imajoh-Ohmi S., Tsutsumi O. et al. (1996) Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. J. Cell Biol. 133: 141-149
    • (1996) J. Cell Biol. , vol.133 , pp. 141-149
    • Takai, Y.1    Ogawara, M.2    Tomono, Y.3    Moritoh, C.4    Imajoh-Ohmi, S.5    Tsutsumi, O.6
  • 178
    • 0037018847 scopus 로고    scopus 로고
    • A role for PI 3-kinase and PKB activity in the G2/M phase of the cell cycle
    • Shtivelman E., Sussman J. and Stokoe D. (2002) A role for PI 3-kinase and PKB activity in the G2/M phase of the cell cycle. Curr. Biol. 12: 919-924
    • (2002) Curr. Biol. , vol.12 , pp. 919-924
    • Shtivelman, E.1    Sussman, J.2    Stokoe, D.3
  • 179
    • 0038061468 scopus 로고    scopus 로고
    • Requirement for phosphatidylinositol-3 kinase activity during progression through S-phase and entry into mitosis
    • Dangi S., Cha H. and Shapiro P. (2003) Requirement for phosphatidylinositol-3 kinase activity during progression through S-phase and entry into mitosis. Cell. Signal. 15: 667-675
    • (2003) Cell. Signal. , vol.15 , pp. 667-675
    • Dangi, S.1    Cha, H.2    Shapiro, P.3
  • 180
    • 0036787934 scopus 로고    scopus 로고
    • Distinct cell cycle timing requirements for extracellular signal-regulated kinase and phosphoinositide 3-kinase signaling pathways in somatic cell mitosis
    • Roberts E. C., Shapiro P. S., Nahreini T. S., Pages G., Pouyssegur J. and Ahn N. G. (2002) Distinct cell cycle timing requirements for extracellular signal-regulated kinase and phosphoinositide 3-kinase signaling pathways in somatic cell mitosis. Mol. Cell. Biol. 22: 7226-7241
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7226-7241
    • Roberts, E.C.1    Shapiro, P.S.2    Nahreini, T.S.3    Pages, G.4    Pouyssegur, J.5    Ahn, N.G.6
  • 181
    • 0035909313 scopus 로고    scopus 로고
    • Forkhead transcription factors contribute to execution of the mitotic programme in mammals
    • Alvarez B., Martinez A. C., Burgering B. M. and Carrera A. C. (2001) Forkhead transcription factors contribute to execution of the mitotic programme in mammals. Nature 413: 744-747
    • (2001) Nature , vol.413 , pp. 744-747
    • Alvarez, B.1    Martinez, A.C.2    Burgering, B.M.3    Carrera, A.C.4
  • 182
  • 183
  • 184
    • 0345305711 scopus 로고    scopus 로고
    • Promotion of mitosis by activated protein kinase B after DNA damage involves polo-like kinase 1 and checkpoint protein CHFR
    • Shtivelman E. (2003) Promotion of mitosis by activated protein kinase B after DNA damage involves polo-like kinase 1 and checkpoint protein CHFR. Mol. Cancer Res. 1: 959-969
    • (2003) Mol. Cancer Res. , vol.1 , pp. 959-969
    • Shtivelman, E.1
  • 185
    • 0030308967 scopus 로고    scopus 로고
    • Regulation of Cdc2 activity by phosphorylation at T14/Y15
    • Berry L. D. and Gould K. L. (1996) Regulation of Cdc2 activity by phosphorylation at T14/Y15. Prog. Cell Cycle Res. 2: 99-105
    • (1996) Prog. Cell Cycle Res. , vol.2 , pp. 99-105
    • Berry, L.D.1    Gould, K.L.2
  • 186
    • 21844479572 scopus 로고    scopus 로고
    • Roles of Pdk1p, a fission yeast protein related to phosphoinositide- dependent protein kinase, in the regulation of mitosis and cytokinesis
    • Bimbo A., Liu J. and Balasubramanian M. K. (2005) Roles of Pdk1p, a fission yeast protein related to phosphoinositide-dependent protein kinase, in the regulation of mitosis and cytokinesis. Mol. Biol. Cell 16: 3162-3175
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3162-3175
    • Bimbo, A.1    Liu, J.2    Balasubramanian, M.K.3
  • 187
    • 0035826154 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase
    • Toyoshima-Morimoto F., Taniguchi E., Shinya N., Iwamatsu A. and Nishida E. (2001) Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase. Nature 410: 215-220
    • (2001) Nature , vol.410 , pp. 215-220
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Shinya, N.3    Iwamatsu, A.4    Nishida, E.5
  • 188
    • 0035826155 scopus 로고    scopus 로고
    • Exploring complex networks
    • Strogatz S. H. (2001) Exploring complex networks. Nature 410: 268-276
    • (2001) Nature , vol.410 , pp. 268-276
    • Strogatz, S.H.1
  • 189
    • 7644238181 scopus 로고    scopus 로고
    • Biological robustness
    • Kitano H. (2004) Biological robustness. Nat. Rev. Genet. 5: 826-837
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 826-837
    • Kitano, H.1
  • 191
    • 1842848073 scopus 로고    scopus 로고
    • Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography
    • Camb.
    • Nowakowski J., Cronin C. N., McRee D. E., Knuth M. W., Nelson C. G., Pavletich N. P. et al. (2002) Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure (Camb.) 10: 1659-1667
    • (2002) Structure , vol.10 , pp. 1659-1667
    • Nowakowski, J.1    Cronin, C.N.2    McRee, D.E.3    Knuth, M.W.4    Nelson, C.G.5    Pavletich, N.P.6
  • 192
    • 0037048281 scopus 로고    scopus 로고
    • Centrosomes and checkpoints: The MPS1 family of kinases
    • Winey M. and Huneycutt B. J. (2002) Centrosomes and checkpoints: the MPS1 family of kinases. Oncogene 21: 6161-6169
    • (2002) Oncogene , vol.21 , pp. 6161-6169
    • Winey, M.1    Huneycutt, B.J.2


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