메뉴 건너뛰기




Volumn 1786, Issue 1, 2008, Pages 60-72

The Aurora kinase family in cell division and cancer

Author keywords

Aurora; Cancer; Cell division; Checkpoint; Mitosis

Indexed keywords

AURORA A KINASE; AURORA B KINASE; PROTEIN AURORA C KINASE; UNCLASSIFIED DRUG;

EID: 51649095569     PISSN: 0304419X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbcan.2008.07.003     Document Type: Review
Times cited : (389)

References (219)
  • 1
    • 0035144407 scopus 로고    scopus 로고
    • Re-staging mitosis: a contemporary view of mitotic progression
    • Pines J., and Rieder C.L. Re-staging mitosis: a contemporary view of mitotic progression. Nat. Cell Biol. 3 (2001) E3-6
    • (2001) Nat. Cell Biol. , vol.3
    • Pines, J.1    Rieder, C.L.2
  • 2
    • 33745176774 scopus 로고    scopus 로고
    • Polo-like kinases: a team in control of the division
    • van de Weerdt B.C., and Medema R.H. Polo-like kinases: a team in control of the division. Cell Cycle 5 (2006) 853-864
    • (2006) Cell Cycle , vol.5 , pp. 853-864
    • van de Weerdt, B.C.1    Medema, R.H.2
  • 3
    • 0038739131 scopus 로고    scopus 로고
    • Never say never. The NIMA-related protein kinases in mitotic control
    • O'Connell M.J., Krien M.J., and Hunter T. Never say never. The NIMA-related protein kinases in mitotic control. Trends Cell Biol. 13 (2003) 221-228
    • (2003) Trends Cell Biol. , vol.13 , pp. 221-228
    • O'Connell, M.J.1    Krien, M.J.2    Hunter, T.3
  • 5
    • 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. Mutations in aurora prevent centrosome separation leading to the formation of monopolar spindles. Cell 81 (1995) 95-105
    • (1995) Cell , vol.81 , pp. 95-105
    • Glover, D.M.1    Leibowitz, M.H.2    McLean, D.A.3    Parry, H.4
  • 6
    • 0027515186 scopus 로고
    • Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast
    • Chan C.S., and Botstein D. Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics 135 (1993) 677-691
    • (1993) Genetics , vol.135 , pp. 677-691
    • Chan, C.S.1    Botstein, D.2
  • 7
    • 0028304675 scopus 로고
    • Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation
    • Francisco L., Wang W., and Chan C.S. Type 1 protein phosphatase acts in opposition to IpL1 protein kinase in regulating yeast chromosome segregation. Mol. Cell. Biol. 14 (1994) 4731-4740
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4731-4740
    • Francisco, L.1    Wang, W.2    Chan, C.S.3
  • 8
    • 0035694554 scopus 로고    scopus 로고
    • The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation
    • Petersen J., Paris J., Willer M., Philippe M., and Hagan I.M. The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation. J. Cell. Sci. 114 (2001) 4371-4384
    • (2001) J. Cell. Sci. , vol.114 , pp. 4371-4384
    • Petersen, J.1    Paris, J.2    Willer, M.3    Philippe, M.4    Hagan, I.M.5
  • 9
    • 0030946109 scopus 로고    scopus 로고
    • Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1
    • Kimura M., Kotani S., Hattori T., Sumi N., Yoshioka T., Todokoro K., and Okano Y. Cell cycle-dependent expression and spindle pole localization of a novel human protein kinase, Aik, related to Aurora of Drosophila and yeast Ipl1. J. Biol. Chem. 272 (1997) 13766-13771
    • (1997) J. Biol. Chem. , vol.272 , pp. 13766-13771
    • Kimura, M.1    Kotani, S.2    Hattori, T.3    Sumi, N.4    Yoshioka, T.5    Todokoro, K.6    Okano, Y.7
  • 10
    • 0037155870 scopus 로고    scopus 로고
    • Cell-cycle-dependent regulation of human Aurora A transcription is mediated by periodic repression of E4TF1
    • Tanaka M., Ueda A., Kanamori H., Ideguchi H., Yang J., Kitajima S., and Ishigatsubo Y. Cell-cycle-dependent regulation of human Aurora A transcription is mediated by periodic repression of E4TF1. J. Biol. Chem. 277 (2002) 10719-10726
    • (2002) J. Biol. Chem. , vol.277 , pp. 10719-10726
    • Tanaka, M.1    Ueda, A.2    Kanamori, H.3    Ideguchi, H.4    Yang, J.5    Kitajima, S.6    Ishigatsubo, Y.7
  • 12
    • 28544449224 scopus 로고    scopus 로고
    • Forkhead box M1 regulates the transcriptional network of genes essential for mitotic progression and genes encoding the SCF (Skp2-Cks1) ubiquitin ligase
    • Wang I.C., Chen Y.J., Hughes D., Petrovic V., Major M.L., Park H.J., Tan Y., Ackerson T., and Costa R.H. Forkhead box M1 regulates the transcriptional network of genes essential for mitotic progression and genes encoding the SCF (Skp2-Cks1) ubiquitin ligase. Mol. Cell. Biol. 25 (2005) 10875-10894
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10875-10894
    • Wang, I.C.1    Chen, Y.J.2    Hughes, D.3    Petrovic, V.4    Major, M.L.5    Park, H.J.6    Tan, Y.7    Ackerson, T.8    Costa, R.H.9
  • 13
    • 0035378348 scopus 로고    scopus 로고
    • The zinc finger domain of Tzfp binds to the tbs motif located at the upstream flanking region of the Aie1 (Aurora-C) kinase gene
    • Tang C.J., Chuang C.K., Hu H.M., and Tang T.K. The zinc finger domain of Tzfp binds to the tbs motif located at the upstream flanking region of the Aie1 (Aurora-C) kinase gene. J. Biol. Chem. 276 (2001) 19631-19639
    • (2001) J. Biol. Chem. , vol.276 , pp. 19631-19639
    • Tang, C.J.1    Chuang, C.K.2    Hu, H.M.3    Tang, T.K.4
  • 14
    • 0034717818 scopus 로고    scopus 로고
    • TPX2, a novel Xenopus MAP involved in spindle pole organization
    • Wittmann T., Wilm M., Karsenti E., and Vernos I. TPX2, a novel Xenopus MAP involved in spindle pole organization. J. Cell. Biol. 149 (2000) 1405-1418
    • (2000) J. Cell. Biol. , vol.149 , pp. 1405-1418
    • Wittmann, T.1    Wilm, M.2    Karsenti, E.3    Vernos, I.4
  • 16
    • 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. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol. Cell 12 (2003) 851-862
    • (2003) Mol. Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 17
    • 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. A novel mechanism for activation of the protein kinase Aurora A. Curr. Biol. 13 (2003) 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
  • 18
    • 28444447726 scopus 로고    scopus 로고
    • Aurora A kinase-coated beads function as microtubule-organizing centers and enhance RanGTP-induced spindle assembly
    • Tsai M.Y., and Zheng Y. Aurora A kinase-coated beads function as microtubule-organizing centers and enhance RanGTP-induced spindle assembly. Curr. Biol. 15 (2005) 2156-2163
    • (2005) Curr. Biol. , vol.15 , pp. 2156-2163
    • Tsai, M.Y.1    Zheng, Y.2
  • 19
    • 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., Hatakeyama K., and Saya H. Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Cell 114 (2003) 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    Hatakeyama, K.7    Saya, H.8
  • 21
    • 0037117408 scopus 로고    scopus 로고
    • Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis
    • Berdnik D., and Knoblich J.A. Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis. Curr. Biol. 12 (2002) 640-647
    • (2002) Curr. Biol. , vol.12 , pp. 640-647
    • Berdnik, D.1    Knoblich, J.A.2
  • 22
    • 27144495462 scopus 로고    scopus 로고
    • The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome
    • Pugacheva E.N., and Golemis E.A. The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome. Nat. Cell. Biol. 7 (2005) 937-946
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 937-946
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 23
    • 2942590333 scopus 로고    scopus 로고
    • Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein
    • Satinover D.L., Leach C.A., Stukenberg P.T., and Brautigan D.L. Activation of Aurora-A kinase by protein phosphatase inhibitor-2, a bifunctional signaling protein. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 8625-8630
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8625-8630
    • Satinover, D.L.1    Leach, C.A.2    Stukenberg, P.T.3    Brautigan, D.L.4
  • 25
    • 33845783921 scopus 로고    scopus 로고
    • Chromosomal enrichment and activation of the Aurora B pathway are coupled to spatially regulate spindle assembly
    • Kelly A.E., Sampath S.C., Maniar T.A., Woo E.M., Chait B.T., and Funabiki H. Chromosomal enrichment and activation of the Aurora B pathway are coupled to spatially regulate spindle assembly. Dev. Cell 12 (2007) 31-43
    • (2007) Dev. Cell , vol.12 , pp. 31-43
    • Kelly, A.E.1    Sampath, S.C.2    Maniar, T.A.3    Woo, E.M.4    Chait, B.T.5    Funabiki, H.6
  • 26
    • 33745275629 scopus 로고    scopus 로고
    • The chromosomal passenger complex: guiding Aurora-B through mitosis
    • Vader G., Medema R.H., and Lens S.M. The chromosomal passenger complex: guiding Aurora-B through mitosis. J. Cell. Biol. 173 (2006) 833-837
    • (2006) J. Cell. Biol. , vol.173 , pp. 833-837
    • Vader, G.1    Medema, R.H.2    Lens, S.M.3
  • 29
    • 20144382378 scopus 로고    scopus 로고
    • The C. elegans Tousled-like kinase contributes to chromosome segregation as a substrate and regulator of the Aurora B kinase
    • Han Z., Riefler G.M., Saam J.R., Mango S.E., and Schumacher J.M. The C. elegans Tousled-like kinase contributes to chromosome segregation as a substrate and regulator of the Aurora B kinase. Curr. Biol. 15 (2005) 894-904
    • (2005) Curr. Biol. , vol.15 , pp. 894-904
    • Han, Z.1    Riefler, G.M.2    Saam, J.R.3    Mango, S.E.4    Schumacher, J.M.5
  • 30
    • 45149116480 scopus 로고    scopus 로고
    • Tousled-mediated activation of Aurora B kinase does not require tousled kinase activity in vivo
    • Riefler G.M., Dent S.Y., and Schumacher J.M. Tousled-mediated activation of Aurora B kinase does not require tousled kinase activity in vivo. J. Biol. Chem. 283 (2008) 12763-12768
    • (2008) J. Biol. Chem. , vol.283 , pp. 12763-12768
    • Riefler, G.M.1    Dent, S.Y.2    Schumacher, J.M.3
  • 31
    • 38549168381 scopus 로고    scopus 로고
    • Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation
    • Rosasco-Nitcher S.E., Lan W., Khorasanizadeh S., and Stukenberg P.T. Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation. Science 319 (2008) 469-472
    • (2008) Science , vol.319 , pp. 469-472
    • Rosasco-Nitcher, S.E.1    Lan, W.2    Khorasanizadeh, S.3    Stukenberg, P.T.4
  • 35
    • 20344405716 scopus 로고    scopus 로고
    • Mechanism of Aurora-B degradation and its dependency on intact KEN and A-boxes: identification of an aneuploidy-promoting property
    • Nguyen H.G., Chinnappan D., Urano T., and Ravid K. Mechanism of Aurora-B degradation and its dependency on intact KEN and A-boxes: identification of an aneuploidy-promoting property. Mol. Cell. Biol. 25 (2005) 4977-4992
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4977-4992
    • Nguyen, H.G.1    Chinnappan, D.2    Urano, T.3    Ravid, K.4
  • 36
    • 0035834435 scopus 로고    scopus 로고
    • Identification of a functional destruction box in the Xenopus laevis Aurora-A kinase pEg2
    • Arlot-Bonnemains Y., Klotzbucher A., Giet R., Uzbekov R., Bihan R., and Prigent C. Identification of a functional destruction box in the Xenopus laevis Aurora-A kinase pEg2. FEBS Lett. 508 (2001) 149-152
    • (2001) FEBS Lett. , vol.508 , pp. 149-152
    • Arlot-Bonnemains, Y.1    Klotzbucher, A.2    Giet, R.3    Uzbekov, R.4    Bihan, R.5    Prigent, C.6
  • 37
    • 12344309497 scopus 로고    scopus 로고
    • Requirements for the destruction of human Aurora-A
    • Crane R., Kloepfer A., and Ruderman J.V. Requirements for the destruction of human Aurora-A. J. Cell. Sci. 117 (2004) 5975-5983
    • (2004) J. Cell. Sci. , vol.117 , pp. 5975-5983
    • Crane, R.1    Kloepfer, A.2    Ruderman, J.V.3
  • 38
    • 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. 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 (2002) 2274-2285
    • (2002) Genes Dev. , vol.16 , pp. 2274-2285
    • Littlepage, L.E.1    Ruderman, J.V.2
  • 39
    • 25444493567 scopus 로고    scopus 로고
    • Destruction box-dependent degradation of Aurora B is mediated by the anaphase-promoting complex/cyclosome and Cdh1
    • Stewart S., and Fang G. Destruction box-dependent degradation of Aurora B is mediated by the anaphase-promoting complex/cyclosome and Cdh1. Cancer Res. 65 (2005) 8730-8735
    • (2005) Cancer Res. , vol.65 , pp. 8730-8735
    • Stewart, S.1    Fang, G.2
  • 40
    • 34249305132 scopus 로고    scopus 로고
    • A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells
    • Sumara I., Quadroni M., Frei C., Olma M.H., Sumara G., Ricci R., and Peter M. A Cul3-based E3 ligase removes Aurora B from mitotic chromosomes, regulating mitotic progression and completion of cytokinesis in human cells. Dev. Cell 12 (2007) 887-900
    • (2007) Dev. Cell , vol.12 , pp. 887-900
    • Sumara, I.1    Quadroni, M.2    Frei, C.3    Olma, M.H.4    Sumara, G.5    Ricci, R.6    Peter, M.7
  • 41
    • 37549068963 scopus 로고    scopus 로고
    • Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
    • Ramadan K., Bruderer R., Spiga F.M., Popp O., Baur T., Gotta M., and Meyer H.H. Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin. Nature 450 (2007) 1258-1262
    • (2007) Nature , vol.450 , pp. 1258-1262
    • Ramadan, K.1    Bruderer, R.2    Spiga, F.M.3    Popp, O.4    Baur, T.5    Gotta, M.6    Meyer, H.H.7
  • 42
    • 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. The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A. Mol. Cell 20 (2005) 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
  • 43
    • 32244446180 scopus 로고    scopus 로고
    • A functional interplay between Aurora-A, Plk1 and TPX2 at spindle poles: Plk1 controls centrosomal localization of Aurora-A and TPX2 spindle association
    • De Luca M., Lavia P., and Guarguaglini G. A functional interplay between Aurora-A, Plk1 and TPX2 at spindle poles: Plk1 controls centrosomal localization of Aurora-A and TPX2 spindle association. Cell Cycle 5 (2006) 296-303
    • (2006) Cell Cycle , vol.5 , pp. 296-303
    • De Luca, M.1    Lavia, P.2    Guarguaglini, G.3
  • 44
    • 33645525342 scopus 로고    scopus 로고
    • The PITSLRE/CDK11p58 protein kinase promotes centrosome maturation and bipolar spindle formation
    • Petretti C., Savoian M., Montembault E., Glover D.M., Prigent C., and Giet R. The PITSLRE/CDK11p58 protein kinase promotes centrosome maturation and bipolar spindle formation. EMBO Rep. 7 (2006) 418-424
    • (2006) EMBO Rep. , vol.7 , pp. 418-424
    • Petretti, C.1    Savoian, M.2    Montembault, E.3    Glover, D.M.4    Prigent, C.5    Giet, R.6
  • 45
    • 0041885288 scopus 로고    scopus 로고
    • Interaction of Aurora-A and centrosomin at the microtubule-nucleating site in Drosophila and mammalian cells
    • Terada Y., Uetake Y., and Kuriyama R. Interaction of Aurora-A and centrosomin at the microtubule-nucleating site in Drosophila and mammalian cells. J. Cell. Biol. 162 (2003) 757-763
    • (2003) J. Cell. Biol. , vol.162 , pp. 757-763
    • Terada, Y.1    Uetake, Y.2    Kuriyama, R.3
  • 48
    • 31444456040 scopus 로고    scopus 로고
    • LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis
    • Abe Y., Ohsugi M., Haraguchi K., Fujimoto J., and Yamamoto T. LATS2-Ajuba complex regulates gamma-tubulin recruitment to centrosomes and spindle organization during mitosis. FEBS Lett. 580 (2006) 782-788
    • (2006) FEBS Lett. , vol.580 , pp. 782-788
    • Abe, Y.1    Ohsugi, M.2    Haraguchi, K.3    Fujimoto, J.4    Yamamoto, T.5
  • 49
    • 25444485717 scopus 로고    scopus 로고
    • Aurora A activates D-TACC-Msps complexes exclusively at centrosomes to stabilize centrosomal microtubules
    • Barros T.P., Kinoshita K., Hyman A.A., and Raff J.W. Aurora A activates D-TACC-Msps complexes exclusively at centrosomes to stabilize centrosomal microtubules. J. Cell. Biol. 170 (2005) 1039-1046
    • (2005) J. Cell. Biol. , vol.170 , pp. 1039-1046
    • Barros, T.P.1    Kinoshita, K.2    Hyman, A.A.3    Raff, J.W.4
  • 50
    • 0037017398 scopus 로고    scopus 로고
    • Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
    • Giet R., McLean D., Descamps S., Lee M.J., Raff J.W., Prigent C., and Glover D.M. Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules. J. Cell. Biol. 156 (2002) 437-451
    • (2002) J. Cell. Biol. , vol.156 , pp. 437-451
    • Giet, R.1    McLean, D.2    Descamps, S.3    Lee, M.J.4    Raff, J.W.5    Prigent, C.6    Glover, D.M.7
  • 51
    • 0035945342 scopus 로고    scopus 로고
    • Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans
    • Hannak E., Kirkham M., Hyman A.A., and Oegema K. Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans. J. Cell. Biol. 155 (2001) 1109-1116
    • (2001) J. Cell. Biol. , vol.155 , pp. 1109-1116
    • Hannak, E.1    Kirkham, M.2    Hyman, A.A.3    Oegema, K.4
  • 52
    • 33645823588 scopus 로고    scopus 로고
    • Aurora A, mitotic entry, and spindle bipolarity
    • Liu Q., and Ruderman J.V. Aurora A, mitotic entry, and spindle bipolarity. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 5811-5816
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 5811-5816
    • Liu, Q.1    Ruderman, J.V.2
  • 53
    • 0031938231 scopus 로고    scopus 로고
    • The Xenopus protein kinase pEg2 associates with the centrosome in a cell cycle-dependent manner, binds to the spindle microtubules and is involved in bipolar mitotic spindle assembly
    • Roghi C., Giet R., Uzbekov R., Morin N., Chartrain I., Le Guellec R., Couturier A., Doree M., Philippe M., and Prigent C. The Xenopus protein kinase pEg2 associates with the centrosome in a cell cycle-dependent manner, binds to the spindle microtubules and is involved in bipolar mitotic spindle assembly. J. Cell. Sci. 111 Pt 5 (1998) 557-572
    • (1998) J. Cell. Sci. , vol.111 , Issue.PART 5 , pp. 557-572
    • Roghi, C.1    Giet, R.2    Uzbekov, R.3    Morin, N.4    Chartrain, I.5    Le Guellec, R.6    Couturier, A.7    Doree, M.8    Philippe, M.9    Prigent, C.10
  • 54
    • 0033591432 scopus 로고    scopus 로고
    • The Xenopus laevis aurora-related protein kinase pEg2 associates with and phosphorylates the kinesin-related protein XlEg5
    • Giet R., Uzbekov R., Cubizolles F., Le Guellec K., and Prigent C. The Xenopus laevis aurora-related protein kinase pEg2 associates with and phosphorylates the kinesin-related protein XlEg5. J. Biol. Chem. 274 (1999) 15005-15013
    • (1999) J. Biol. Chem. , vol.274 , pp. 15005-15013
    • Giet, R.1    Uzbekov, R.2    Cubizolles, F.3    Le Guellec, K.4    Prigent, C.5
  • 55
    • 0033971720 scopus 로고    scopus 로고
    • Centrosome-independent mitotic spindle formation in vertebrates
    • Khodjakov A., Cole R.W., Oakley B.R., and Rieder C.L. Centrosome-independent mitotic spindle formation in vertebrates. Curr. Biol. 10 (2000) 59-67
    • (2000) Curr. Biol. , vol.10 , pp. 59-67
    • Khodjakov, A.1    Cole, R.W.2    Oakley, B.R.3    Rieder, C.L.4
  • 56
    • 10344231994 scopus 로고    scopus 로고
    • Kinetochore-driven formation of kinetochore fibers contributes to spindle assembly during animal mitosis
    • Maiato H., Rieder C.L., and Khodjakov A. Kinetochore-driven formation of kinetochore fibers contributes to spindle assembly during animal mitosis. J. Cell. Biol. 167 (2004) 831-840
    • (2004) J. Cell. Biol. , vol.167 , pp. 831-840
    • Maiato, H.1    Rieder, C.L.2    Khodjakov, A.3
  • 57
    • 0033536178 scopus 로고    scopus 로고
    • Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation
    • Carazo-Salas R.E., Guarguaglini G., Gruss O.J., Segref A., Karsenti E., and Mattaj I.W. Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation. Nature 400 (1999) 178-181
    • (1999) Nature , vol.400 , pp. 178-181
    • Carazo-Salas, R.E.1    Guarguaglini, G.2    Gruss, O.J.3    Segref, A.4    Karsenti, E.5    Mattaj, I.W.6
  • 58
    • 0033591373 scopus 로고    scopus 로고
    • Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran
    • Wilde A., and Zheng Y. Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran. Science 284 (1999) 1359-1362
    • (1999) Science , vol.284 , pp. 1359-1362
    • Wilde, A.1    Zheng, Y.2
  • 59
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • Kalab P., Weis K., and Heald R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science 295 (2002) 2452-2456
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 60
    • 33645452992 scopus 로고    scopus 로고
    • Analysis of a RanGTP-regulated gradient in mitotic somatic cells
    • Kalab P., Pralle A., Isacoff E.Y., Heald R., and Weis K. Analysis of a RanGTP-regulated gradient in mitotic somatic cells. Nature 440 (2006) 697-701
    • (2006) Nature , vol.440 , pp. 697-701
    • Kalab, P.1    Pralle, A.2    Isacoff, E.Y.3    Heald, R.4    Weis, K.5
  • 61
    • 23944436962 scopus 로고    scopus 로고
    • Spatial coordination of spindle assembly by chromosome-mediated signaling gradients
    • Caudron M., Bunt G., Bastiaens P., and Karsenti E. Spatial coordination of spindle assembly by chromosome-mediated signaling gradients. Science 309 (2005) 1373-1376
    • (2005) Science , vol.309 , pp. 1373-1376
    • Caudron, M.1    Bunt, G.2    Bastiaens, P.3    Karsenti, E.4
  • 63
    • 0035951480 scopus 로고    scopus 로고
    • Role of importin-beta in coupling Ran to downstream targets in microtubule assembly
    • Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., and Zheng Y. Role of importin-beta in coupling Ran to downstream targets in microtubule assembly. Science 291 (2001) 653-656
    • (2001) Science , vol.291 , pp. 653-656
    • Wiese, C.1    Wilde, A.2    Moore, M.S.3    Adam, S.A.4    Merdes, A.5    Zheng, Y.6
  • 65
    • 17444411537 scopus 로고    scopus 로고
    • A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly
    • Blower M.D., Nachury M., Heald R., and Weis K. A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. Cell 121 (2005) 223-234
    • (2005) Cell , vol.121 , pp. 223-234
    • Blower, M.D.1    Nachury, M.2    Heald, R.3    Weis, K.4
  • 69
    • 33749598020 scopus 로고    scopus 로고
    • Aurora-A kinase and inhibitor-2 regulate the cyclin threshold for mitotic entry in Xenopus early embryonic cell cycles
    • Satinover D.L., Brautigan D.L., and Stukenberg P.T. Aurora-A kinase and inhibitor-2 regulate the cyclin threshold for mitotic entry in Xenopus early embryonic cell cycles. Cell Cycle 5 (2006) 2268-2274
    • (2006) Cell Cycle , vol.5 , pp. 2268-2274
    • Satinover, D.L.1    Brautigan, D.L.2    Stukenberg, P.T.3
  • 71
    • 46249084662 scopus 로고    scopus 로고
    • Bora and the kinase Aurora A cooperatively activate the kinase Plk1 and control mitotic entry
    • Seki A., Coppinger J.A., Jang C.Y., Yates J.R., and Fang G. Bora and the kinase Aurora A cooperatively activate the kinase Plk1 and control mitotic entry. Science 320 (2008) 1655-1658
    • (2008) Science , vol.320 , pp. 1655-1658
    • Seki, A.1    Coppinger, J.A.2    Jang, C.Y.3    Yates, J.R.4    Fang, G.5
  • 72
    • 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. Polo-like kinase-1 controls recovery from a G2 DNA damage-induced arrest in mammalian cells. Mol. Cell 15 (2004) 799-811
    • (2004) Mol. Cell , vol.15 , pp. 799-811
    • van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 73
    • 23844494690 scopus 로고    scopus 로고
    • Restarting the cell cycle when the checkpoint comes to a halt
    • van Vugt M.A., Bras A., and Medema R.H. Restarting the cell cycle when the checkpoint comes to a halt. Cancer Res. 65 (2005) 7037-7040
    • (2005) Cancer Res. , vol.65 , pp. 7037-7040
    • van Vugt, M.A.1    Bras, A.2    Medema, R.H.3
  • 74
    • 25444470823 scopus 로고    scopus 로고
    • CDC25B phosphorylation by Aurora-A occurs at the G2/M transition and is inhibited by DNA damage
    • Cazales M., Schmitt E., Montembault E., Dozier C., Prigent C., and Ducommun B. CDC25B phosphorylation by Aurora-A occurs at the G2/M transition and is inhibited by DNA damage. Cell Cycle 4 (2005) 1233-1238
    • (2005) Cell Cycle , vol.4 , pp. 1233-1238
    • Cazales, M.1    Schmitt, E.2    Montembault, E.3    Dozier, C.4    Prigent, C.5    Ducommun, B.6
  • 75
    • 26444493574 scopus 로고    scopus 로고
    • Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1-Cdk1 at the centrosome
    • Lindqvist A., Kallstrom H., Lundgren A., Barsoum E., and Rosenthal C.K. Cdc25B cooperates with Cdc25A to induce mitosis but has a unique role in activating cyclin B1-Cdk1 at the centrosome. J. Cell Biol. 171 (2005) 35-45
    • (2005) J. Cell Biol. , vol.171 , pp. 35-45
    • Lindqvist, A.1    Kallstrom, H.2    Lundgren, A.3    Barsoum, E.4    Rosenthal, C.K.5
  • 76
    • 33846211025 scopus 로고    scopus 로고
    • Sensory cilia and integration of signal transduction in human health and disease
    • Christensen S.T., Pedersen L.B., Schneider L., and Satir P. Sensory cilia and integration of signal transduction in human health and disease. Traffic 8 (2007) 97-109
    • (2007) Traffic , vol.8 , pp. 97-109
    • Christensen, S.T.1    Pedersen, L.B.2    Schneider, L.3    Satir, P.4
  • 77
    • 33645220356 scopus 로고    scopus 로고
    • HEF1-Aurora A interactions: points of dialog between the cell cycle and cell attachment signaling networks
    • Pugacheva E.N., and Golemis E.A. HEF1-Aurora A interactions: points of dialog between the cell cycle and cell attachment signaling networks. Cell Cycle 5 (2006) 384-391
    • (2006) Cell Cycle , vol.5 , pp. 384-391
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 78
    • 0037349338 scopus 로고    scopus 로고
    • The making of the mitotic chromosome: modern insights into classical questions
    • Swedlow J.R., and Hirano T. The making of the mitotic chromosome: modern insights into classical questions. Mol. Cell 11 (2003) 557-569
    • (2003) Mol. Cell , vol.11 , pp. 557-569
    • Swedlow, J.R.1    Hirano, T.2
  • 79
    • 33646177549 scopus 로고    scopus 로고
    • At the heart of the chromosome: SMC proteins in action
    • Hirano T. At the heart of the chromosome: SMC proteins in action. Nat. Rev., Mol. Cell Biol. 7 (2006) 311-322
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 311-322
    • Hirano, T.1
  • 80
    • 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. 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 (2001) 669-682
    • (2001) J. Cell Biol. , vol.152 , pp. 669-682
    • Giet, R.1    Glover, D.M.2
  • 81
    • 33750036679 scopus 로고    scopus 로고
    • Molecular analysis of mitotic chromosome condensation using a quantitative time-resolved fluorescence microscopy assay
    • Maddox P.S., Portier N., Desai A., and Oegema K. Molecular analysis of mitotic chromosome condensation using a quantitative time-resolved fluorescence microscopy assay. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 15097-15102
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15097-15102
    • Maddox, P.S.1    Portier, N.2    Desai, A.3    Oegema, K.4
  • 82
    • 34248179475 scopus 로고    scopus 로고
    • Aurora B controls the association of Condensin I but not Condensin II with mitotic chromosomes
    • Lipp J.J., Hirota T., Poser I., and Peters J.M. Aurora B controls the association of Condensin I but not Condensin II with mitotic chromosomes. J. Cell. Sci. 120 (2007) 1245-1255
    • (2007) J. Cell. Sci. , vol.120 , pp. 1245-1255
    • Lipp, J.J.1    Hirota, T.2    Poser, I.3    Peters, J.M.4
  • 84
    • 0036896143 scopus 로고    scopus 로고
    • Cohesin release is required for sister chromatid resolution, but not for Condensin-mediated compaction, at the onset of mitosis
    • Losada A., Hirano M., and Hirano T. Cohesin release is required for sister chromatid resolution, but not for Condensin-mediated compaction, at the onset of mitosis. Genes Dev. 16 (2002) 3004-3016
    • (2002) Genes Dev. , vol.16 , pp. 3004-3016
    • Losada, A.1    Hirano, M.2    Hirano, T.3
  • 85
    • 0034820448 scopus 로고    scopus 로고
    • Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair
    • Morishita J., Matsusaka T., Goshima G., Nakamura T., Tatebe H., and Yanagida M. Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair. Genes Cells 6 (2001) 743-763
    • (2001) Genes Cells , vol.6 , pp. 743-763
    • Morishita, J.1    Matsusaka, T.2    Goshima, G.3    Nakamura, T.4    Tatebe, H.5    Yanagida, M.6
  • 86
    • 3042809666 scopus 로고    scopus 로고
    • Spatial and temporal regulation of Condensins I and II in mitotic chromosome assembly in human cells
    • Ono T., Fang Y., Spector D.L., and Hirano T. Spatial and temporal regulation of Condensins I and II in mitotic chromosome assembly in human cells. Mol. Biol. Cell 15 (2004) 3296-3308
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3296-3308
    • Ono, T.1    Fang, Y.2    Spector, D.L.3    Hirano, T.4
  • 87
    • 0035858865 scopus 로고    scopus 로고
    • Essential roles of Drosophila inner centromere protein (INCENP) and Aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation
    • Adams R.R., Maiato H., Earnshaw W.C., and Carmena M. Essential roles of Drosophila inner centromere protein (INCENP) and Aurora B in histone H3 phosphorylation, metaphase chromosome alignment, kinetochore disjunction, and chromosome segregation. J. Cell Biol. 153 (2001) 865-880
    • (2001) J. Cell Biol. , vol.153 , pp. 865-880
    • Adams, R.R.1    Maiato, H.2    Earnshaw, W.C.3    Carmena, M.4
  • 89
    • 0032560517 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena
    • Wei Y., Mizzen C.A., Cook R.G., Gorovsky M.A., and Allis C.D. Phosphorylation of histone H3 at serine 10 is correlated with chromosome condensation during mitosis and meiosis in Tetrahymena. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 7480-7484
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7480-7484
    • Wei, Y.1    Mizzen, C.A.2    Cook, R.G.3    Gorovsky, M.A.4    Allis, C.D.5
  • 90
    • 0142136096 scopus 로고    scopus 로고
    • Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3
    • Mellone B.G., Ball L., Suka N., Grunstein M.R., Partridge J.F., and Allshire R.C. Centromere silencing and function in fission yeast is governed by the amino terminus of histone H3. Curr. Biol. 13 (2003) 1748-1757
    • (2003) Curr. Biol. , vol.13 , pp. 1748-1757
    • Mellone, B.G.1    Ball, L.2    Suka, N.3    Grunstein, M.R.4    Partridge, J.F.5    Allshire, R.C.6
  • 91
    • 28844475262 scopus 로고    scopus 로고
    • Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
    • Hirota T., Lipp J.J., Toh B.H., and Peters J.M. Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin. Nature 438 (2005) 1176-1180
    • (2005) Nature , vol.438 , pp. 1176-1180
    • Hirota, T.1    Lipp, J.J.2    Toh, B.H.3    Peters, J.M.4
  • 93
    • 22244481613 scopus 로고    scopus 로고
    • The structure and function of SMC and kleisin complexes
    • Nasmyth K., and Haering C.H. The structure and function of SMC and kleisin complexes. Annu. Rev. Biochem. 74 (2005) 595-648
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 595-648
    • Nasmyth, K.1    Haering, C.H.2
  • 94
    • 0035230592 scopus 로고    scopus 로고
    • Splitting the chromosome: cutting the ties that bind sister chromatids
    • discussion 133-118, 158-163
    • Nasmyth K., Peters J.M., and Uhlmann F. Splitting the chromosome: cutting the ties that bind sister chromatids. Novartis Found Symp. 237 (2001) 113-133 discussion 133-118, 158-163
    • (2001) Novartis Found Symp. , vol.237 , pp. 113-133
    • Nasmyth, K.1    Peters, J.M.2    Uhlmann, F.3
  • 95
    • 0034721656 scopus 로고    scopus 로고
    • Two distinct pathways remove mammalian Cohesin from chromosome arms in prophase and from centromeres in anaphase
    • Waizenegger I.C., Hauf S., Meinke A., and Peters J.M. Two distinct pathways remove mammalian Cohesin from chromosome arms in prophase and from centromeres in anaphase. Cell 103 (2000) 399-410
    • (2000) Cell , vol.103 , pp. 399-410
    • Waizenegger, I.C.1    Hauf, S.2    Meinke, A.3    Peters, J.M.4
  • 98
    • 0028972048 scopus 로고
    • Mei-S332, a Drosophila protein required for sister-chromatid Cohesion, can localize to meiotic centromere regions
    • Kerrebrock A.W., Moore D.P., Wu J.S., and Orr-Weaver T.L. Mei-S332, a Drosophila protein required for sister-chromatid Cohesion, can localize to meiotic centromere regions. Cell 83 (1995) 247-256
    • (1995) Cell , vol.83 , pp. 247-256
    • Kerrebrock, A.W.1    Moore, D.P.2    Wu, J.S.3    Orr-Weaver, T.L.4
  • 99
    • 1142298825 scopus 로고    scopus 로고
    • The conserved kinetochore protein Shugoshin protects centromeric cohesion during meiosis
    • Kitajima T.S., Kawashima S.A., and Watanabe Y. The conserved kinetochore protein Shugoshin protects centromeric cohesion during meiosis. Nature 427 (2004) 510-517
    • (2004) Nature , vol.427 , pp. 510-517
    • Kitajima, T.S.1    Kawashima, S.A.2    Watanabe, Y.3
  • 102
    • 18044393595 scopus 로고    scopus 로고
    • Dissociation of Cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2
    • Hauf S., Roitinger E., Koch B., Dittrich C.M., Mechtler K., and Peters J.M. Dissociation of Cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2. PLoS Biol. 3 (2005) e69
    • (2005) PLoS Biol. , vol.3
    • Hauf, S.1    Roitinger, E.2    Koch, B.3    Dittrich, C.M.4    Mechtler, K.5    Peters, J.M.6
  • 103
    • 33646098667 scopus 로고    scopus 로고
    • PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation
    • Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., and Yu H. PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation. Dev. Cell 10 (2006) 575-585
    • (2006) Dev. Cell , vol.10 , pp. 575-585
    • Tang, Z.1    Shu, H.2    Qi, W.3    Mahmood, N.A.4    Mumby, M.C.5    Yu, H.6
  • 104
    • 4444224967 scopus 로고    scopus 로고
    • Vertebrate Shugoshin links sister centromere cohesion and kinetochore microtubule stability in mitosis
    • Salic A., Waters J.C., and Mitchison T.J. Vertebrate Shugoshin links sister centromere cohesion and kinetochore microtubule stability in mitosis. Cell 118 (2004) 567-578
    • (2004) Cell , vol.118 , pp. 567-578
    • Salic, A.1    Waters, J.C.2    Mitchison, T.J.3
  • 105
    • 18044394368 scopus 로고    scopus 로고
    • Shugoshin prevents dissociation of Cohesin from centromeres during mitosis in vertebrate cells
    • McGuinness B.E., Hirota T., Kudo N.R., Peters J.M., and Nasmyth K. Shugoshin prevents dissociation of Cohesin from centromeres during mitosis in vertebrate cells. PLoS Biol. 3 (2005) e86
    • (2005) PLoS Biol. , vol.3
    • McGuinness, B.E.1    Hirota, T.2    Kudo, N.R.3    Peters, J.M.4    Nasmyth, K.5
  • 106
    • 33750428233 scopus 로고    scopus 로고
    • Regulation of mitotic chromosome cohesion by Haspin and Aurora B
    • Dai J., Sullivan B.A., and Higgins J.M. Regulation of mitotic chromosome cohesion by Haspin and Aurora B. Dev. Cell 11 (2006) 741-750
    • (2006) Dev. Cell , vol.11 , pp. 741-750
    • Dai, J.1    Sullivan, B.A.2    Higgins, J.M.3
  • 107
    • 33745653601 scopus 로고    scopus 로고
    • INCENP and Aurora B promote meiotic sister chromatid cohesion through localization of the Shugoshin MEI-S332 in Drosophila
    • Resnick T.D., Satinover D.L., MacIsaac F., Stukenberg P.T., Earnshaw W.C., Orr-Weaver T.L., and Carmena M. INCENP and Aurora B promote meiotic sister chromatid cohesion through localization of the Shugoshin MEI-S332 in Drosophila. Dev. Cell 11 (2006) 57-68
    • (2006) Dev. Cell , vol.11 , pp. 57-68
    • Resnick, T.D.1    Satinover, D.L.2    MacIsaac, F.3    Stukenberg, P.T.4    Earnshaw, W.C.5    Orr-Weaver, T.L.6    Carmena, M.7
  • 110
    • 3242657509 scopus 로고    scopus 로고
    • The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly
    • Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., and Funabiki H. The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly. Cell 118 (2004) 187-202
    • (2004) Cell , vol.118 , pp. 187-202
    • Sampath, S.C.1    Ohi, R.2    Leismann, O.3    Salic, A.4    Pozniakovski, A.5    Funabiki, H.6
  • 111
    • 34548481992 scopus 로고    scopus 로고
    • Aurora B phosphorylates multiple sites on MCAK to spatially and temporally regulate its function
    • Zhang X., Lan W., Ems-McClung S.C., Stukenberg P.T., and Walczak C.E. Aurora B phosphorylates multiple sites on MCAK to spatially and temporally regulate its function. Mol. Biol. Cell (2008) 3264-3276
    • (2008) Mol. Biol. Cell , pp. 3264-3276
    • Zhang, X.1    Lan, W.2    Ems-McClung, S.C.3    Stukenberg, P.T.4    Walczak, C.E.5
  • 112
    • 33644746123 scopus 로고    scopus 로고
    • Molecular requirements for kinetochore-associated microtubule formation in mammalian cells
    • Tulu U.S., Fagerstrom C., Ferenz N.P., and Wadsworth P. Molecular requirements for kinetochore-associated microtubule formation in mammalian cells. Curr. Biol. 16 (2006) 536-541
    • (2006) Curr. Biol. , vol.16 , pp. 536-541
    • Tulu, U.S.1    Fagerstrom, C.2    Ferenz, N.P.3    Wadsworth, P.4
  • 113
    • 33645231284 scopus 로고    scopus 로고
    • Aurora B is required for mitotic chromatin-induced phosphorylation of Op18/Stathmin
    • Gadea B.B., and Ruderman J.V. Aurora B is required for mitotic chromatin-induced phosphorylation of Op18/Stathmin. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4493-4498
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4493-4498
    • Gadea, B.B.1    Ruderman, J.V.2
  • 114
    • 0037459109 scopus 로고    scopus 로고
    • Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling
    • Cleveland D.W., Mao Y., and Sullivan K.F. Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling. Cell 112 (2003) 407-421
    • (2003) Cell , vol.112 , pp. 407-421
    • Cleveland, D.W.1    Mao, Y.2    Sullivan, K.F.3
  • 115
    • 12344289259 scopus 로고    scopus 로고
    • Kinetochore-spindle microtubule interactions during mitosis
    • Kline-Smith S.L., Sandall S., and Desai A. Kinetochore-spindle microtubule interactions during mitosis. Curr. Opin. Cell Biol. 17 (2005) 35-46
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 35-46
    • Kline-Smith, S.L.1    Sandall, S.2    Desai, A.3
  • 117
    • 0017259847 scopus 로고
    • Light and electron microscopy of rat kangaroo cells in mitosis. III. Patterns of chromosome behavior during prometaphase
    • Roos U.P. Light and electron microscopy of rat kangaroo cells in mitosis. III. Patterns of chromosome behavior during prometaphase. Chromosoma 54 (1976) 363-385
    • (1976) Chromosoma , vol.54 , pp. 363-385
    • Roos, U.P.1
  • 118
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E., Stark M.J., and Nasmyth K. Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections. Cell 108 (2002) 317-329
    • (2002) Cell , vol.108 , pp. 317-329
    • Tanaka, T.U.1    Rachidi, N.2    Janke, C.3    Pereira, G.4    Galova, M.5    Schiebel, E.6    Stark, M.J.7    Nasmyth, K.8
  • 121
    • 1542399869 scopus 로고    scopus 로고
    • Correcting improper chromosome-spindle attachments during cell division
    • Lampson M.A., Renduchitala K., Khodjakov A., and Kapoor T.M. Correcting improper chromosome-spindle attachments during cell division. Nat. Cell Biol. 6 (2004) 232-237
    • (2004) Nat. Cell Biol. , vol.6 , pp. 232-237
    • Lampson, M.A.1    Renduchitala, K.2    Khodjakov, A.3    Kapoor, T.M.4
  • 124
    • 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. Differentiation of cytoplasmic and meiotic spindle assembly MCAK functions by Aurora B-dependent phosphorylation. Mol. Biol. Cell 15 (2004) 2895-2906
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2895-2906
    • Ohi, R.1    Sapra, T.2    Howard, J.3    Mitchison, T.J.4
  • 125
    • 33751232957 scopus 로고    scopus 로고
    • The conserved KMN network constitutes the core microtubule-binding site of the kinetochore
    • Cheeseman I.M., Chappie J.S., Wilson-Kubalek E.M., and Desai A. The conserved KMN network constitutes the core microtubule-binding site of the kinetochore. Cell 127 (2006) 983-997
    • (2006) Cell , vol.127 , pp. 983-997
    • Cheeseman, I.M.1    Chappie, J.S.2    Wilson-Kubalek, E.M.3    Desai, A.4
  • 126
    • 33751227843 scopus 로고    scopus 로고
    • Kinetochore microtubule dynamics and attachment stability are regulated by Hec1
    • DeLuca J.G., Gall W.E., Ciferri C., Cimini D., Musacchio A., and Salmon E.D. Kinetochore microtubule dynamics and attachment stability are regulated by Hec1. Cell 127 (2006) 969-982
    • (2006) Cell , vol.127 , pp. 969-982
    • DeLuca, J.G.1    Gall, W.E.2    Ciferri, C.3    Cimini, D.4    Musacchio, A.5    Salmon, E.D.6
  • 127
    • 0035972237 scopus 로고    scopus 로고
    • Merotelic kinetochore orientation is a major mechanism of aneuploidy in mitotic mammalian tissue cells
    • Cimini D., Howell B., Maddox P., Khodjakov A., Degrassi F., and Salmon E.D. Merotelic kinetochore orientation is a major mechanism of aneuploidy in mitotic mammalian tissue cells. J. Cell Biol. 153 (2001) 517-527
    • (2001) J. Cell Biol. , vol.153 , pp. 517-527
    • Cimini, D.1    Howell, B.2    Maddox, P.3    Khodjakov, A.4    Degrassi, F.5    Salmon, E.D.6
  • 128
    • 0242287897 scopus 로고    scopus 로고
    • Merotelic kinetochore orientation occurs frequently during early mitosis in mammalian tissue cells and error correction is achieved by two different mechanisms
    • Cimini D., Moree B., Canman J.C., and Salmon E.D. Merotelic kinetochore orientation occurs frequently during early mitosis in mammalian tissue cells and error correction is achieved by two different mechanisms. J. Cell. Sci. 116 (2003) 4213-4225
    • (2003) J. Cell. Sci. , vol.116 , pp. 4213-4225
    • Cimini, D.1    Moree, B.2    Canman, J.C.3    Salmon, E.D.4
  • 130
    • 33750612373 scopus 로고    scopus 로고
    • Aurora kinase promotes turnover of kinetochore microtubules to reduce chromosome segregation errors
    • Cimini D., Wan X., Hirel C.B., and Salmon E.D. Aurora kinase promotes turnover of kinetochore microtubules to reduce chromosome segregation errors. Curr. Biol. 16 (2006) 1711-1718
    • (2006) Curr. Biol. , vol.16 , pp. 1711-1718
    • Cimini, D.1    Wan, X.2    Hirel, C.B.3    Salmon, E.D.4
  • 131
    • 33750609316 scopus 로고    scopus 로고
    • Aurora B is enriched at merotelic attachment sites, where it regulates MCAK
    • Knowlton A.L., Lan W., and Stukenberg P.T. Aurora B is enriched at merotelic attachment sites, where it regulates MCAK. Curr. Biol. 16 (2006) 1705-1710
    • (2006) Curr. Biol. , vol.16 , pp. 1705-1710
    • Knowlton, A.L.1    Lan, W.2    Stukenberg, P.T.3
  • 132
    • 0041941573 scopus 로고    scopus 로고
    • An inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin
    • Ohi R., Coughlin M.L., Lane W.S., and Mitchison T.J. An inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin. Dev. Cell 5 (2003) 309-321
    • (2003) Dev. Cell , vol.5 , pp. 309-321
    • Ohi, R.1    Coughlin, M.L.2    Lane, W.S.3    Mitchison, T.J.4
  • 134
    • 34247333444 scopus 로고    scopus 로고
    • The spindle-assembly checkpoint in space and time
    • Musacchio A., and Salmon E.D. The spindle-assembly checkpoint in space and time. Nat. Rev., Mol. Cell Biol. 8 (2007) 379-393
    • (2007) Nat. Rev., Mol. Cell Biol. , vol.8 , pp. 379-393
    • Musacchio, A.1    Salmon, E.D.2
  • 135
    • 0027942033 scopus 로고
    • Anaphase onset in vertebrate somatic cells is controlled by a checkpoint that monitors sister kinetochore attachment to the spindle
    • Rieder C.L., Schultz A., Cole R., and Sluder G. Anaphase onset in vertebrate somatic cells is controlled by a checkpoint that monitors sister kinetochore attachment to the spindle. J. Cell Biol. 127 (1994) 1301-1310
    • (1994) J. Cell Biol. , vol.127 , pp. 1301-1310
    • Rieder, C.L.1    Schultz, A.2    Cole, R.3    Sluder, G.4
  • 136
    • 0029160299 scopus 로고
    • The checkpoint delaying anaphase in response to chromosome monoorientation is mediated by an inhibitory signal produced by unattached kinetochores
    • Rieder C.L., Cole R.W., Khodjakov A., and Sluder G. The checkpoint delaying anaphase in response to chromosome monoorientation is mediated by an inhibitory signal produced by unattached kinetochores. J. Cell Biol. 130 (1995) 941-948
    • (1995) J. Cell Biol. , vol.130 , pp. 941-948
    • Rieder, C.L.1    Cole, R.W.2    Khodjakov, A.3    Sluder, G.4
  • 137
    • 0026009964 scopus 로고
    • Feedback control of mitosis in budding yeast
    • Li R., and Murray A.W. Feedback control of mitosis in budding yeast. Cell 66 (1991) 519-531
    • (1991) Cell , vol.66 , pp. 519-531
    • Li, R.1    Murray, A.W.2
  • 138
    • 0025941405 scopus 로고
    • S. cerevisiae genes required for cell cycle arrest in response to loss of microtubule function
    • Hoyt M.A., Totis L., and Roberts B.T. S. cerevisiae genes required for cell cycle arrest in response to loss of microtubule function. Cell 66 (1991) 507-517
    • (1991) Cell , vol.66 , pp. 507-517
    • Hoyt, M.A.1    Totis, L.2    Roberts, B.T.3
  • 139
    • 0030066347 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint
    • Weiss E., and Winey M. The Saccharomyces cerevisiae spindle pole body duplication gene MPS1 is part of a mitotic checkpoint. J. Cell Biol. 132 (1996) 111-123
    • (1996) J. Cell Biol. , vol.132 , pp. 111-123
    • Weiss, E.1    Winey, M.2
  • 140
    • 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., Ruderman J.V., and Hershko A. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Biol. Cell 6 (1995) 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    Ruderman, J.V.7    Hershko, A.8
  • 141
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B
    • King R.W., Peters J.M., Tugendreich S., Rolfe M., Hieter P., and Kirschner M.W. A 20S complex containing CDC27 and CDC16 catalyzes the mitosis-specific conjugation of ubiquitin to cyclin B. Cell 81 (1995) 279-288
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 142
    • 0029033504 scopus 로고
    • Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast
    • Irniger S., Piatti S., Michaelis C., and Nasmyth K. Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast. Cell 81 (1995) 269-278
    • (1995) Cell , vol.81 , pp. 269-278
    • Irniger, S.1    Piatti, S.2    Michaelis, C.3    Nasmyth, K.4
  • 143
    • 0030839209 scopus 로고    scopus 로고
    • The anaphase-promoting complex is required in G1 arrested yeast cells to inhibit B-type cyclin accumulation and to prevent uncontrolled entry into S-phase
    • Irniger S., and Nasmyth K. The anaphase-promoting complex is required in G1 arrested yeast cells to inhibit B-type cyclin accumulation and to prevent uncontrolled entry into S-phase. J. Cell. Sci. 110 Pt 13 (1997) 1523-1531
    • (1997) J. Cell. Sci. , vol.110 , Issue.PART 13 , pp. 1523-1531
    • Irniger, S.1    Nasmyth, K.2
  • 144
    • 0032511150 scopus 로고    scopus 로고
    • An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast
    • Ciosk R., Zachariae W., Michaelis C., Shevchenko A., Mann M., and Nasmyth K. An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast. Cell 93 (1998) 1067-1076
    • (1998) Cell , vol.93 , pp. 1067-1076
    • Ciosk, R.1    Zachariae, W.2    Michaelis, C.3    Shevchenko, A.4    Mann, M.5    Nasmyth, K.6
  • 145
    • 0344578064 scopus 로고    scopus 로고
    • APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5
    • Shirayama M., Toth A., Galova M., and Nasmyth K. APC(Cdc20) promotes exit from mitosis by destroying the anaphase inhibitor Pds1 and cyclin Clb5. Nature 402 (1999) 203-207
    • (1999) Nature , vol.402 , pp. 203-207
    • Shirayama, M.1    Toth, A.2    Galova, M.3    Nasmyth, K.4
  • 146
    • 0030693087 scopus 로고    scopus 로고
    • CDC20 and CDH1: a family of substrate-specific activators of APC-dependent proteolysis
    • Visintin R., Prinz S., and Amon A. CDC20 and CDH1: a family of substrate-specific activators of APC-dependent proteolysis. Science 278 (1997) 460-463
    • (1997) Science , vol.278 , pp. 460-463
    • Visintin, R.1    Prinz, S.2    Amon, A.3
  • 147
    • 33747589184 scopus 로고    scopus 로고
    • The anaphase promoting complex/cyclosome: a machine designed to destroy
    • Peters J.M. The anaphase promoting complex/cyclosome: a machine designed to destroy. Nat. Rev., Mol. Cell Biol. 7 (2006) 644-656
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 644-656
    • Peters, J.M.1
  • 148
    • 0035802122 scopus 로고    scopus 로고
    • Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2
    • Sudakin V., Chan G.K., and Yen T.J. Checkpoint inhibition of the APC/C in HeLa cells is mediated by a complex of BUBR1, BUB3, CDC20, and MAD2. J. Cell Biol. 154 (2001) 925-936
    • (2001) J. Cell Biol. , vol.154 , pp. 925-936
    • Sudakin, V.1    Chan, G.K.2    Yen, T.J.3
  • 149
    • 0036797033 scopus 로고    scopus 로고
    • Mad2 and BubR1 function in a single checkpoint pathway that responds to a loss of tension
    • Shannon K.B., Canman J.C., and Salmon E.D. Mad2 and BubR1 function in a single checkpoint pathway that responds to a loss of tension. Mol. Biol. Cell 13 (2002) 3706-3719
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3706-3719
    • Shannon, K.B.1    Canman, J.C.2    Salmon, E.D.3
  • 151
    • 0032101688 scopus 로고    scopus 로고
    • Localization of Mad2 to kinetochores depends on microtubule attachment, not tension
    • Waters J.C., Chen R.H., Murray A.W., and Salmon E.D. Localization of Mad2 to kinetochores depends on microtubule attachment, not tension. J. Cell. Biol. 141 (1998) 1181-1191
    • (1998) J. Cell. Biol. , vol.141 , pp. 1181-1191
    • Waters, J.C.1    Chen, R.H.2    Murray, A.W.3    Salmon, E.D.4
  • 152
    • 0028872743 scopus 로고
    • Mitotic forces control a cell-cycle checkpoint
    • Li X., and Nicklas R.B. Mitotic forces control a cell-cycle checkpoint. Nature 373 (1995) 630-632
    • (1995) Nature , vol.373 , pp. 630-632
    • Li, X.1    Nicklas, R.B.2
  • 153
    • 14444267778 scopus 로고    scopus 로고
    • How cells get the right chromosomes
    • Nicklas R.B. How cells get the right chromosomes. Science 275 (1997) 632-637
    • (1997) Science , vol.275 , pp. 632-637
    • Nicklas, R.B.1
  • 154
    • 24344439888 scopus 로고    scopus 로고
    • The spindle checkpoint: tension versus attachment
    • Pinsky B.A., and Biggins S. The spindle checkpoint: tension versus attachment. Trends Cell Biol. 15 (2005) 486-493
    • (2005) Trends Cell Biol. , vol.15 , pp. 486-493
    • Pinsky, B.A.1    Biggins, S.2
  • 155
    • 0035577762 scopus 로고    scopus 로고
    • The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint
    • Biggins S., and Murray A.W. The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint. Genes Dev. 15 (2001) 3118-3129
    • (2001) Genes Dev. , vol.15 , pp. 3118-3129
    • Biggins, S.1    Murray, A.W.2
  • 157
    • 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., Heckel A., van Meel J., Rieder C.L., and Peters J.M. 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 (2003) 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    Heckel, A.7    van Meel, J.8    Rieder, C.L.9    Peters, J.M.10
  • 159
    • 0042170180 scopus 로고    scopus 로고
    • Survivin is required for stable checkpoint activation in taxol-treated HeLa cells
    • Carvalho A., Carmena M., Sambade C., Earnshaw W.C., and Wheatley S.P. Survivin is required for stable checkpoint activation in taxol-treated HeLa cells. J. Cell. Sci. 116 (2003) 2987-2998
    • (2003) J. Cell. Sci. , vol.116 , pp. 2987-2998
    • Carvalho, A.1    Carmena, M.2    Sambade, C.3    Earnshaw, W.C.4    Wheatley, S.P.5
  • 160
    • 35848971221 scopus 로고    scopus 로고
    • The chromosomal passenger complex controls spindle checkpoint function independent from its role in correcting microtubule kinetochore interactions
    • Vader G., Cruijsen C.W., van Harn T., Vromans M.J., Medema R.H., and Lens S.M. The chromosomal passenger complex controls spindle checkpoint function independent from its role in correcting microtubule kinetochore interactions. Mol. Biol. Cell 18 (2007) 4553-4564
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4553-4564
    • Vader, G.1    Cruijsen, C.W.2    van Harn, T.3    Vromans, M.J.4    Medema, R.H.5    Lens, S.M.6
  • 161
    • 30344462087 scopus 로고    scopus 로고
    • The Ipl1-Aurora protein kinase activates the spindle checkpoint by creating unattached kinetochores
    • Pinsky B.A., Kung C., Shokat K.M., and Biggins S. The Ipl1-Aurora protein kinase activates the spindle checkpoint by creating unattached kinetochores. Nat. Cell Biol. 8 (2006) 78-83
    • (2006) Nat. Cell Biol. , vol.8 , pp. 78-83
    • Pinsky, B.A.1    Kung, C.2    Shokat, K.M.3    Biggins, S.4
  • 162
    • 0037018844 scopus 로고    scopus 로고
    • Inhibition of Aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
    • Kallio M.J., McCleland M.L., Stukenberg P.T., and Gorbsky G.J. Inhibition of Aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis. Curr. Biol. 12 (2002) 900-905
    • (2002) Curr. Biol. , vol.12 , pp. 900-905
    • Kallio, M.J.1    McCleland, M.L.2    Stukenberg, P.T.3    Gorbsky, G.J.4
  • 163
    • 4444249610 scopus 로고    scopus 로고
    • Kinetochore localization of spindle checkpoint proteins: who controls whom?
    • Vigneron S., Prieto S., Bernis C., Labbe J.C., Castro A., and Lorca T. Kinetochore localization of spindle checkpoint proteins: who controls whom?. Mol. Biol. Cell 15 (2004) 4584-4596
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4584-4596
    • Vigneron, S.1    Prieto, S.2    Bernis, C.3    Labbe, J.C.4    Castro, A.5    Lorca, T.6
  • 164
    • 0037380133 scopus 로고    scopus 로고
    • S. pombe aurora kinase/Survivin is required for chromosome condensation and the spindle checkpoint attachment response
    • Petersen J., and Hagan I.M. S. pombe aurora kinase/Survivin is required for chromosome condensation and the spindle checkpoint attachment response. Curr. Biol. 13 (2003) 590-597
    • (2003) Curr. Biol. , vol.13 , pp. 590-597
    • Petersen, J.1    Hagan, I.M.2
  • 165
    • 34249106861 scopus 로고    scopus 로고
    • Ipl1p-dependent phosphorylation of Mad3p is required for the spindle checkpoint response to lack of tension at kinetochores
    • King E.M., Rachidi N., Morrice N., Hardwick K.G., and Stark M.J. Ipl1p-dependent phosphorylation of Mad3p is required for the spindle checkpoint response to lack of tension at kinetochores. Genes Dev. 21 (2007) 1163-1168
    • (2007) Genes Dev. , vol.21 , pp. 1163-1168
    • King, E.M.1    Rachidi, N.2    Morrice, N.3    Hardwick, K.G.4    Stark, M.J.5
  • 166
    • 34548436939 scopus 로고    scopus 로고
    • Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions
    • Elowe S., Hummer S., Uldschmid A., Li X., and Nigg E.A. Tension-sensitive Plk1 phosphorylation on BubR1 regulates the stability of kinetochore microtubule interactions. Genes Dev. 21 (2007) 2205-2219
    • (2007) Genes Dev. , vol.21 , pp. 2205-2219
    • Elowe, S.1    Hummer, S.2    Uldschmid, A.3    Li, X.4    Nigg, E.A.5
  • 167
    • 0033677801 scopus 로고    scopus 로고
    • Tension on chromosomes increases the number of kinetochore microtubules but only within limits
    • King J.M., and Nicklas R.B. Tension on chromosomes increases the number of kinetochore microtubules but only within limits. J. Cell. Sci. 113 Pt 21 (2000) 3815-3823
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 21 , pp. 3815-3823
    • King, J.M.1    Nicklas, R.B.2
  • 168
    • 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. AIM-1: a mammalian midbody-associated protein required for cytokinesis. Embo J. 17 (1998) 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
  • 169
    • 0037076212 scopus 로고    scopus 로고
    • The Aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous chromosomes during meiosis
    • Kaitna S., Pasierbek P., Jantsch M., Loidl J., and Glotzer M. The Aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous chromosomes during meiosis. Curr. Biol. 12 (2002) 798-812
    • (2002) Curr. Biol. , vol.12 , pp. 798-812
    • Kaitna, S.1    Pasierbek, P.2    Jantsch, M.3    Loidl, J.4    Glotzer, M.5
  • 170
    • 0034609763 scopus 로고    scopus 로고
    • The aurora-related kinase AIR-2 recruits ZEN-4/CeMKLP1 to the mitotic spindle at metaphase and is required for cytokinesis
    • Severson A.F., Hamill D.R., Carter J.C., Schumacher J., and Bowerman B. The aurora-related kinase AIR-2 recruits ZEN-4/CeMKLP1 to the mitotic spindle at metaphase and is required for cytokinesis. Curr. Biol. 10 (2000) 1162-1171
    • (2000) Curr. Biol. , vol.10 , pp. 1162-1171
    • Severson, A.F.1    Hamill, D.R.2    Carter, J.C.3    Schumacher, J.4    Bowerman, B.5
  • 171
    • 12744261490 scopus 로고    scopus 로고
    • Stabilization of microtubule dynamics at anaphase onset promotes chromosome segregation
    • Higuchi T., and Uhlmann F. Stabilization of microtubule dynamics at anaphase onset promotes chromosome segregation. Nature 433 (2005) 171-176
    • (2005) Nature , vol.433 , pp. 171-176
    • Higuchi, T.1    Uhlmann, F.2
  • 172
    • 0037415571 scopus 로고    scopus 로고
    • The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly
    • Buvelot S., Tatsutani S.Y., Vermaak D., and Biggins S. The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly. J. Cell Biol. 160 (2003) 329-339
    • (2003) J. Cell Biol. , vol.160 , pp. 329-339
    • Buvelot, S.1    Tatsutani, S.Y.2    Vermaak, D.3    Biggins, S.4
  • 173
    • 15244356577 scopus 로고    scopus 로고
    • The molecular requirements for cytokinesis
    • Glotzer M. The molecular requirements for cytokinesis. Science 307 (2005) 1735-1739
    • (2005) Science , vol.307 , pp. 1735-1739
    • Glotzer, M.1
  • 174
  • 175
    • 23944499922 scopus 로고    scopus 로고
    • An ECT2-centralspindlin complex regulates the localization and function of RhoA
    • Yuce O., Piekny A., and Glotzer M. An ECT2-centralspindlin complex regulates the localization and function of RhoA. J. Cell Biol. 170 (2005) 571-582
    • (2005) J. Cell Biol. , vol.170 , pp. 571-582
    • Yuce, O.1    Piekny, A.2    Glotzer, M.3
  • 176
    • 31644438188 scopus 로고    scopus 로고
    • Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis
    • Nishimura Y., and Yonemura S. Centralspindlin regulates ECT2 and RhoA accumulation at the equatorial cortex during cytokinesis. J. Cell. Sci. 119 (2006) 104-114
    • (2006) J. Cell. Sci. , vol.119 , pp. 104-114
    • Nishimura, Y.1    Yonemura, S.2
  • 177
    • 24944480674 scopus 로고    scopus 로고
    • MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis
    • Zhao W.M., and Fang G. MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13158-13163
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13158-13163
    • Zhao, W.M.1    Fang, G.2
  • 178
    • 0027103924 scopus 로고
    • The pebble gene is required for cytokinesis in Drosophila
    • Lehner C.F. The pebble gene is required for cytokinesis in Drosophila. J. Cell. Sci. 103 Pt 4 (1992) 1021-1030
    • (1992) J. Cell. Sci. , vol.103 , Issue.PART 4 , pp. 1021-1030
    • Lehner, C.F.1
  • 179
    • 0033615978 scopus 로고    scopus 로고
    • Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis
    • Tatsumoto T., Xie X., Blumenthal R., Okamoto I., and Miki T. Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis. J. Cell Biol. 147 (1999) 921-928
    • (1999) J. Cell Biol. , vol.147 , pp. 921-928
    • Tatsumoto, T.1    Xie, X.2    Blumenthal, R.3    Okamoto, I.4    Miki, T.5
  • 180
    • 0034609747 scopus 로고    scopus 로고
    • Incenp and an aurora-like kinase form a complex essential for chromosome segregation and efficient completion of cytokinesis
    • Kaitna S., Mendoza M., Jantsch-Plunger V., and Glotzer M. Incenp and an aurora-like kinase form a complex essential for chromosome segregation and efficient completion of cytokinesis. Curr. Biol. 10 (2000) 1172-1181
    • (2000) Curr. Biol. , vol.10 , pp. 1172-1181
    • Kaitna, S.1    Mendoza, M.2    Jantsch-Plunger, V.3    Glotzer, M.4
  • 181
    • 18044371706 scopus 로고    scopus 로고
    • Phosphorylation of ZEN-4/MKLP1 by Aurora B regulates completion of cytokinesis
    • Guse A., Mishima M., and Glotzer M. Phosphorylation of ZEN-4/MKLP1 by Aurora B regulates completion of cytokinesis. Curr. Biol. 15 (2005) 778-786
    • (2005) Curr. Biol. , vol.15 , pp. 778-786
    • Guse, A.1    Mishima, M.2    Glotzer, M.3
  • 183
    • 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., Nagata K., and Inagaki M. Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J. Biol. Chem. 278 (2003) 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    Nagata, K.7    Inagaki, M.8
  • 184
  • 185
    • 0038371015 scopus 로고    scopus 로고
    • Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase
    • Kawajiri A., Yasui Y., Goto H., Tatsuka M., Takahashi M., Nagata K., and Inagaki M. Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinatedly with Rho-kinase. Mol. Biol. Cell 14 (2003) 1489-1500
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1489-1500
    • Kawajiri, A.1    Yasui, Y.2    Goto, H.3    Tatsuka, M.4    Takahashi, M.5    Nagata, K.6    Inagaki, M.7
  • 186
    • 33645968660 scopus 로고    scopus 로고
    • The NoCut pathway links completion of cytokinesis to spindle midzone function to prevent chromosome breakage
    • Norden C., Mendoza M., Dobbelaere J., Kotwaliwale C.V., Biggins S., and Barral Y. The NoCut pathway links completion of cytokinesis to spindle midzone function to prevent chromosome breakage. Cell 125 (2006) 85-98
    • (2006) Cell , vol.125 , pp. 85-98
    • Norden, C.1    Mendoza, M.2    Dobbelaere, J.3    Kotwaliwale, C.V.4    Biggins, S.5    Barral, Y.6
  • 187
    • 0032212717 scopus 로고    scopus 로고
    • Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter
    • Bernard M., Sanseau P., Henry C., Couturier A., and Prigent C. Cloning of STK13, a third human protein kinase related to Drosophila aurora and budding yeast Ipl1 that maps on chromosome 19q13.3-ter. Genomics 53 (1998) 406-409
    • (1998) Genomics , vol.53 , pp. 406-409
    • Bernard, M.1    Sanseau, P.2    Henry, C.3    Couturier, A.4    Prigent, C.5
  • 188
    • 0033548619 scopus 로고    scopus 로고
    • Cell cycle-dependent expression and centrosome localization of a third human aurora/Ipl1-related protein kinase, AIK3
    • Kimura M., Matsuda Y., Yoshioka T., and Okano Y. Cell cycle-dependent expression and centrosome localization of a third human aurora/Ipl1-related protein kinase, AIK3. J. Biol. Chem. 274 (1999) 7334-7340
    • (1999) J. Biol. Chem. , vol.274 , pp. 7334-7340
    • Kimura, M.1    Matsuda, Y.2    Yoshioka, T.3    Okano, Y.4
  • 189
    • 31544432841 scopus 로고    scopus 로고
    • Dynamic localization and functional implications of Aurora-C kinase during male mouse meiosis
    • Tang C.J., Lin C.Y., and Tang T.K. Dynamic localization and functional implications of Aurora-C kinase during male mouse meiosis. Dev. Biol. 290 (2006) 398-410
    • (2006) Dev. Biol. , vol.290 , pp. 398-410
    • Tang, C.J.1    Lin, C.Y.2    Tang, T.K.3
  • 191
    • 21244481993 scopus 로고    scopus 로고
    • Overexpression of an Aurora-C kinase-deficient mutant disrupts the Aurora-B/INCENP complex and induces polyploidy
    • Chen H.L., Tang C.J., Chen C.Y., and Tang T.K. Overexpression of an Aurora-C kinase-deficient mutant disrupts the Aurora-B/INCENP complex and induces polyploidy. J. Biomed. Sci. 12 (2005) 297-310
    • (2005) J. Biomed. Sci. , vol.12 , pp. 297-310
    • Chen, H.L.1    Tang, C.J.2    Chen, C.Y.3    Tang, T.K.4
  • 192
    • 0031764068 scopus 로고    scopus 로고
    • Protein kinase profile of sperm and eggs: cloning and characterization of two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and fly chromosome segregation regulators
    • Tseng T.C., Chen S.H., Hsu Y.P., and Tang T.K. Protein kinase profile of sperm and eggs: cloning and characterization of two novel testis-specific protein kinases (AIE1, AIE2) related to yeast and fly chromosome segregation regulators. DNA Cell Biol. 17 (1998) 823-833
    • (1998) DNA Cell Biol. , vol.17 , pp. 823-833
    • Tseng, T.C.1    Chen, S.H.2    Hsu, Y.P.3    Tang, T.K.4
  • 195
    • 0038341158 scopus 로고    scopus 로고
    • The Aurora kinases: role in cell transformation and tumorigenesis
    • Katayama H., Brinkley W.R., and Sen S. The Aurora kinases: role in cell transformation and tumorigenesis. Cancer Metastasis Rev. 22 (2003) 451-464
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 451-464
    • Katayama, H.1    Brinkley, W.R.2    Sen, S.3
  • 197
    • 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., Brinkley B.R., and Sen S. Tumour amplified kinase STK15/BTAK induces centrosome amplification, aneuploidy and transformation. Nat. Genet. 20 (1998) 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    Brinkley, B.R.7    Sen, S.8
  • 198
    • 0037084163 scopus 로고    scopus 로고
    • Aurora-A overexpression reveals tetraploidization as a major route to centrosome amplification in p53-/- cells
    • Meraldi P., Honda R., and Nigg E.A. Aurora-A overexpression reveals tetraploidization as a major route to centrosome amplification in p53-/- cells. Embo J. 21 (2002) 483-492
    • (2002) Embo J. , vol.21 , pp. 483-492
    • Meraldi, P.1    Honda, R.2    Nigg, E.A.3
  • 199
    • 0037586498 scopus 로고    scopus 로고
    • AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol
    • Anand S., Penrhyn-Lowe S., and Venkitaraman A.R. AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol. Cancer Cells 3 (2003) 51-62
    • (2003) Cancer Cells , vol.3 , pp. 51-62
    • Anand, S.1    Penrhyn-Lowe, S.2    Venkitaraman, A.R.3
  • 200
    • 13944254035 scopus 로고    scopus 로고
    • Overexpression of Aurora-A potentiates HRAS-mediated oncogenic transformation and is implicated in oral carcinogenesis
    • Tatsuka M., Sato S., Kitajima S., Suto S., Kawai H., Miyauchi M., Ogawa I., Maeda M., Ota T., and Takata T. Overexpression of Aurora-A potentiates HRAS-mediated oncogenic transformation and is implicated in oral carcinogenesis. Oncogene 24 (2005) 1122-1127
    • (2005) Oncogene , vol.24 , pp. 1122-1127
    • Tatsuka, M.1    Sato, S.2    Kitajima, S.3    Suto, S.4    Kawai, H.5    Miyauchi, M.6    Ogawa, I.7    Maeda, M.8    Ota, T.9    Takata, T.10
  • 202
    • 33846811519 scopus 로고    scopus 로고
    • Crosstalk between Aurora-A and p53: frequent deletion or downregulation of Aurora-A in tumors from p53 null mice
    • Mao J.H., Wu D., Perez-Losada J., Jiang T., Li Q., Neve R.M., Gray J.W., Cai W.W., and Balmain A. Crosstalk between Aurora-A and p53: frequent deletion or downregulation of Aurora-A in tumors from p53 null mice. Cancer Cells 11 (2007) 161-173
    • (2007) Cancer Cells , vol.11 , pp. 161-173
    • Mao, J.H.1    Wu, D.2    Perez-Losada, J.3    Jiang, T.4    Li, Q.5    Neve, R.M.6    Gray, J.W.7    Cai, W.W.8    Balmain, A.9
  • 203
    • 0032967120 scopus 로고    scopus 로고
    • Translational control of growth factor and proto-oncogene expression
    • Willis A.E. Translational control of growth factor and proto-oncogene expression. Int. J. Biochem. Cell Biol. 31 (1999) 73-86
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 73-86
    • Willis, A.E.1
  • 205
    • 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., and Cheng J.Q. Aurora-A abrogation of p53 DNA binding and transactivation activity by phosphorylation of serine 215. J. Biol. Chem. 279 (2004) 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    Cheng, J.Q.7
  • 207
    • 1542365225 scopus 로고    scopus 로고
    • Regulation of Xenopus Aurora A activation by TPX2
    • Eyers P.A., and Maller J.L. Regulation of Xenopus Aurora A activation by TPX2. J. Biol. Chem. 279 (2004) 9008-9015
    • (2004) J. Biol. Chem. , vol.279 , pp. 9008-9015
    • Eyers, P.A.1    Maller, J.L.2
  • 208
    • 0037009435 scopus 로고    scopus 로고
    • Suppression of the STK15 oncogenic activity requires a transactivation-independent p53 function
    • Chen S.S., Chang P.C., Cheng Y.W., Tang F.M., and Lin Y.S. Suppression of the STK15 oncogenic activity requires a transactivation-independent p53 function. Embo J. 21 (2002) 4491-4499
    • (2002) Embo J. , vol.21 , pp. 4491-4499
    • Chen, S.S.1    Chang, P.C.2    Cheng, Y.W.3    Tang, F.M.4    Lin, Y.S.5
  • 209
    • 33845702193 scopus 로고    scopus 로고
    • Drosophila Aurora-A kinase inhibits neuroblast self-renewal by regulating aPKC/Numb cortical polarity and spindle orientation
    • Lee C.Y., Andersen R.O., Cabernard C., Manning L., Tran K.D., Lanskey M.J., Bashirullah A., and Doe C.Q. Drosophila Aurora-A kinase inhibits neuroblast self-renewal by regulating aPKC/Numb cortical polarity and spindle orientation. Genes Dev. 20 (2006) 3464-3474
    • (2006) Genes Dev. , vol.20 , pp. 3464-3474
    • Lee, C.Y.1    Andersen, R.O.2    Cabernard, C.3    Manning, L.4    Tran, K.D.5    Lanskey, M.J.6    Bashirullah, A.7    Doe, C.Q.8
  • 210
    • 33845704687 scopus 로고    scopus 로고
    • Aurora-A acts as a tumor suppressor and regulates self-renewal of Drosophila neuroblasts
    • Wang H., Somers G.W., Bashirullah A., Heberlein U., Yu F., and Chia W. Aurora-A acts as a tumor suppressor and regulates self-renewal of Drosophila neuroblasts. Genes Dev. 20 (2006) 3453-3463
    • (2006) Genes Dev. , vol.20 , pp. 3453-3463
    • Wang, H.1    Somers, G.W.2    Bashirullah, A.3    Heberlein, U.4    Yu, F.5    Chia, W.6
  • 211
    • 0037105758 scopus 로고    scopus 로고
    • Increased mitotic phosphorylation of histone H3 attributable to AIM-1/Aurora-B overexpression contributes to chromosome number instability
    • Ota T., Suto S., Katayama H., Han Z.B., Suzuki F., Maeda M., Tanino M., Terada Y., and Tatsuka M. Increased mitotic phosphorylation of histone H3 attributable to AIM-1/Aurora-B overexpression contributes to chromosome number instability. Cancer Res. 62 (2002) 5168-5177
    • (2002) Cancer Res. , vol.62 , pp. 5168-5177
    • Ota, T.1    Suto, S.2    Katayama, H.3    Han, Z.B.4    Suzuki, F.5    Maeda, M.6    Tanino, M.7    Terada, Y.8    Tatsuka, M.9
  • 212
    • 27744511262 scopus 로고    scopus 로고
    • Aurora-B/AIM-1 kinase activity is involved in Ras-mediated cell transformation
    • Kanda A., Kawai H., Suto S., Kitajima S., Sato S., Takata T., and Tatsuka M. Aurora-B/AIM-1 kinase activity is involved in Ras-mediated cell transformation. Oncogene 24 (2005) 7266-7272
    • (2005) Oncogene , vol.24 , pp. 7266-7272
    • Kanda, A.1    Kawai, H.2    Suto, S.3    Kitajima, S.4    Sato, S.5    Takata, T.6    Tatsuka, M.7
  • 213
    • 39149089275 scopus 로고    scopus 로고
    • Polo and Aurora kinases: lessons derived from chemical biology
    • Taylor S., and Peters J.M. Polo and Aurora kinases: lessons derived from chemical biology. Curr. Opin. Cell Biol. 20 (2008) 77-84
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 77-84
    • Taylor, S.1    Peters, J.M.2
  • 215
    • 35548935096 scopus 로고    scopus 로고
    • Limiting the proliferation of polyploid cells
    • Ganem N.J., and Pellman D. Limiting the proliferation of polyploid cells. Cell 131 (2007) 437-440
    • (2007) Cell , vol.131 , pp. 437-440
    • Ganem, N.J.1    Pellman, D.2
  • 217
    • 34250201840 scopus 로고    scopus 로고
    • MLN8054, a small-molecule inhibitor of Aurora A, causes spindle pole and chromosome congression defects leading to aneuploidy
    • Hoar K., Chakravarty A., Rabino C., Wysong D., Bowman D., Roy N., and Ecsedy J.A. MLN8054, a small-molecule inhibitor of Aurora A, causes spindle pole and chromosome congression defects leading to aneuploidy. Mol. Cell. Biol. 27 (2007) 4513-4525
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4513-4525
    • Hoar, K.1    Chakravarty, A.2    Rabino, C.3    Wysong, D.4    Bowman, D.5    Roy, N.6    Ecsedy, J.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.