메뉴 건너뛰기




Volumn 15, Issue 6, 2003, Pages 672-683

Mitotic mechanics: The auroras come into view

Author keywords

[No Author keywords available]

Indexed keywords

AURORA A KINASE; AURORA B KINASE; AURORA KINASE; GUANOSINE TRIPHOSPHATASE; KINESIN; KINESIN LIKE PROTEIN; PHOSPHOTRANSFERASE; PROTEIN; UNCLASSIFIED DRUG;

EID: 0344845010     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2003.10.013     Document Type: Review
Times cited : (263)

References (91)
  • 1
    • 0035945342 scopus 로고    scopus 로고
    • Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans
    • Hannak E., Kirkham M., Hyman A.A., 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
  • 2
    • 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., 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
  • 3
    • 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., Kuriyama R. Interaction of Aurora-A and centrosomin at the microtubule-nucleating site in Drosophila and mammalian cells. J. Cell. Biol. 162:2003;757-764.
    • (2003) J. Cell. Biol. , vol.162 , pp. 757-764
    • Terada, Y.1    Uetake, Y.2    Kuriyama, R.3
  • 4
    • 0037117408 scopus 로고    scopus 로고
    • Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis
    • Berdnik D., 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
  • 5
    • 0037446847 scopus 로고    scopus 로고
    • A novel mechanism for activation of the protein kinase Aurora A
    • The results presented here indicate that Aurora A activation can be mediated by TPX2, which inhibits protein phosphatase 1 access to Aurora A, allowing activation of the kinase by autophosphorylation.
    • Eyers P.A., Erikson E., Chen L.G., Maller J.L. A novel mechanism for activation of the protein kinase Aurora A. Curr. Biol. 13:2003;691-697 The results presented here indicate that Aurora A activation can be mediated by TPX2, which inhibits protein phosphatase 1 access to Aurora A, allowing activation of the kinase by autophosphorylation.
    • (2003) Curr. Biol. , vol.13 , pp. 691-697
    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
  • 6
    • 0037341906 scopus 로고    scopus 로고
    • A Ran signalling pathway mediated by the mitotic kinase Aurora A in spindle assembly
    • This paper reports the interesting finding that TPX2-mediated activation of Aurora A kinase is stimulated by RanGTP in mitotic Xenopus egg extracts. RanGTP is generated by a chromatin-bound exchange factor, therefore linking the activation of Aurora A and control of spindle assembly to the presence of mitotic chromatin.
    • Tsai M.Y., Wiese C., Cao K., Martin O., Donovan P., Ruderman J., Prigent C., Zheng Y. A Ran signalling pathway mediated by the mitotic kinase Aurora A in spindle assembly. Nat. Cell. Biol. 5:2003;242-248 This paper reports the interesting finding that TPX2-mediated activation of Aurora A kinase is stimulated by RanGTP in mitotic Xenopus egg extracts. RanGTP is generated by a chromatin-bound exchange factor, therefore linking the activation of Aurora A and control of spindle assembly to the presence of mitotic chromatin.
    • (2003) Nat. Cell. Biol. , vol.5 , pp. 242-248
    • Tsai, M.Y.1    Wiese, C.2    Cao, K.3    Martin, O.4    Donovan, P.5    Ruderman, J.6    Prigent, C.7    Zheng, Y.8
  • 8
    • 0037048279 scopus 로고    scopus 로고
    • On the role of Aurora-A in centrosome function
    • Dutertre S., Descamps S., Prigent C. On the role of Aurora-A in centrosome function. Oncogene. 21:2002;6175-6183.
    • (2002) Oncogene , vol.21 , pp. 6175-6183
    • Dutertre, S.1    Descamps, S.2    Prigent, C.3
  • 9
    • 0037084163 scopus 로고    scopus 로고
    • -/- cells
    • These authors demonstrate that a major pathway of centrosome amplification in cells overexpressing Aurora A is through a failure of these cells to undergo cytokinesis, rather than a direct effect on centrosome replication.
    • -/- cells. EMBO J. 21:2002;483-492 These authors demonstrate that a major pathway of centrosome amplification in cells overexpressing Aurora A is through a failure of these cells to undergo cytokinesis, rather than a direct effect on centrosome replication.
    • (2002) EMBO J. , vol.21 , pp. 483-492
    • Meraldi, P.1    Honda, R.2    Nigg, E.A.3
  • 10
    • 0037586498 scopus 로고    scopus 로고
    • AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol
    • This paper reports that overexpression of Aurora A, which is common in several forms of cancer, causes polyploidy due to defective cytokinesis following the abolition of the spindle assembly checkpoint.
    • Anand S., Penrhyn-Lowe S., Venkitaraman A.R. AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol. Cancer Cell. 3:2003;51-62 This paper reports that overexpression of Aurora A, which is common in several forms of cancer, causes polyploidy due to defective cytokinesis following the abolition of the spindle assembly checkpoint.
    • (2003) Cancer Cell. , vol.3 , pp. 51-62
    • Anand, S.1    Penrhyn-Lowe, S.2    Venkitaraman, A.R.3
  • 12
    • 0037044846 scopus 로고    scopus 로고
    • Crystal structure of aurora-2, an oncogenic serine/threonine kinase
    • The first crystal structure of an Aurora family kinase reveals certain features that may be employed in the design of specific inhibitors, possibly for use in cancer chemotherapy.
    • Cheetham G.M., Knegtel R.M., Coll J.T., Renwick S.B., Swenson L., Weber P., Lippke J.A., Austen D.A. Crystal structure of aurora-2, an oncogenic serine/threonine kinase. J. Biol. Chem. 277:2002;42419-42422 The first crystal structure of an Aurora family kinase reveals certain features that may be employed in the design of specific inhibitors, possibly for use in cancer chemotherapy.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42419-42422
    • Cheetham, G.M.1    Knegtel, R.M.2    Coll, J.T.3    Renwick, S.B.4    Swenson, L.5    Weber, P.6    Lippke, J.A.7    Austen, D.A.8
  • 13
    • 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., Lees E. The mitotic serine/threonine kinase Aurora2/AIK is regulated by phosphorylation and degradation. Oncogene. 19:2000;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
  • 14
    • 0034213929 scopus 로고    scopus 로고
    • Degradation of human Aurora2 protein kinase by the anaphase-promoting complex-ubiquitin-proteasome pathway
    • Honda K., Mihara H., Kato Y., Yamaguchi A., Tanaka H., Yasuda H., Furukawa K., Urano T. Degradation of human Aurora2 protein kinase by the anaphase-promoting complex-ubiquitin-proteasome pathway. Oncogene. 19:2000;2812-2819.
    • (2000) Oncogene , vol.19 , pp. 2812-2819
    • Honda, K.1    Mihara, H.2    Kato, Y.3    Yamaguchi, A.4    Tanaka, H.5    Yasuda, H.6    Furukawa, K.7    Urano, T.8
  • 15
    • 0035252654 scopus 로고    scopus 로고
    • Chromosomal passengers and the (aurora) ABCs of mitosis
    • Adams R.R., Carmena M., Earnshaw W.C. Chromosomal passengers and the (aurora) ABCs of mitosis. Trends Cell. Biol. 11:2001;49-54.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 49-54
    • Adams, R.R.1    Carmena, M.2    Earnshaw, W.C.3
  • 17
    • 0038070181 scopus 로고    scopus 로고
    • CSC-1: A subunit of the Aurora B kinase complex that binds to the Survivin-like protein BIR-1 and the Incenp-like protein ICP-1
    • A new member of the Aurora B complex is identified and function analysed in C. elegans.
    • Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., Glotzer M. CSC-1: a subunit of the Aurora B kinase complex that binds to the Survivin-like protein BIR-1 and the Incenp-like protein ICP-1. J. Cell. Biol. 161:2003;229-236 A new member of the Aurora B complex is identified and function analysed in C. elegans.
    • (2003) J. Cell. Biol. , vol.161 , pp. 229-236
    • Romano, A.1    Guse, A.2    Krascenicova, I.3    Schnabel, H.4    Schnabel, R.5    Glotzer, M.6
  • 18
    • 0033637849 scopus 로고    scopus 로고
    • The survivin-like C. elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone
    • Speliotes E.K., Uren A., Vaux D., Horvitz H.R. The survivin-like C. elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone. Mol. Cell. 6:2000;211-223.
    • (2000) Mol. Cell. , vol.6 , pp. 211-223
    • Speliotes, E.K.1    Uren, A.2    Vaux, D.3    Horvitz, H.R.4
  • 19
    • 0041778335 scopus 로고    scopus 로고
    • The mammalian passenger protein TD-60 is an RCC1 family member with an essential role in prometaphase-to-metaphase progression
    • This study finally reveals the identity of the TD-60 antigen, a chromosome passenger protein that has been known for many years to colocalise with the Aurora B complex. Intriguingly TD-60 is related to RCC1 and is required for progression from prometaphase to metaphase. TD-60 RNAi leads to loss of Aurora B and survivin from centromeres. TD-60 appears to act as a Rac-specific exchange factor, raising the fascinating possibility that small GTPases regulate Aurora B function at the centromere and the spindle midzone.
    • Mollinari C., Reynaud C., Martineau-Thuillier S., Monier S., Kieffer S., Garin J., Andreassen P.R., Boulet A., Goud B., Kleman J.P., et al. The mammalian passenger protein TD-60 is an RCC1 family member with an essential role in prometaphase-to-metaphase progression. Dev. Cell. 5:2003;295-307 This study finally reveals the identity of the TD-60 antigen, a chromosome passenger protein that has been known for many years to colocalise with the Aurora B complex. Intriguingly TD-60 is related to RCC1 and is required for progression from prometaphase to metaphase. TD-60 RNAi leads to loss of Aurora B and survivin from centromeres. TD-60 appears to act as a Rac-specific exchange factor, raising the fascinating possibility that small GTPases regulate Aurora B function at the centromere and the spindle midzone.
    • (2003) Dev. Cell. , vol.5 , pp. 295-307
    • Mollinari, C.1    Reynaud, C.2    Martineau-Thuillier, S.3    Monier, S.4    Kieffer, S.5    Garin, J.6    Andreassen, P.R.7    Boulet, A.8    Goud, B.9    Kleman, J.P.10
  • 20
    • 0027515186 scopus 로고
    • Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast
    • Chan C.S., 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
  • 21
    • 0033612557 scopus 로고    scopus 로고
    • Sli15 associates with the ipl1 protein kinase to promote proper chromosome segregation in Saccharomyces cerevisiae
    • Kim J.H., Kang J.S., Chan C.S. Sli15 associates with the ipl1 protein kinase to promote proper chromosome segregation in Saccharomyces cerevisiae. J. Cell. Biol. 145:1999;1381-1394.
    • (1999) J. Cell. Biol. , vol.145 , pp. 1381-1394
    • Kim, J.H.1    Kang, J.S.2    Chan, C.S.3
  • 22
    • 0037131572 scopus 로고    scopus 로고
    • Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p
    • Comprehensive study of yeast kinetochore regulation, including purification and characterisation of central and outer kinetochore subcomplexes by mass spectrometry, identification of their in vivo and in vitro phosphorylation sites and functional analysis of the phosphorylation.
    • Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J., Yates J.R. III, Chan C.S., Drubin D.G., Barnes G. Phospho-regulation of kinetochore- microtubule attachments by the Aurora kinase Ipl1p. Cell. 111:2002;163-172 Comprehensive study of yeast kinetochore regulation, including purification and characterisation of central and outer kinetochore subcomplexes by mass spectrometry, identification of their in vivo and in vitro phosphorylation sites and functional analysis of the phosphorylation.
    • (2002) Cell , vol.111 , pp. 163-172
    • Cheeseman, I.M.1    Anderson, S.2    Jwa, M.3    Green, E.M.4    Kang, J.5    Yates III, J.R.6    Chan, C.S.7    Drubin, D.G.8    Barnes, G.9
  • 23
    • 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., Murray A.W. The conserved protein kinase Ipl1 regulates microtubule binding to kinetochores in budding yeast. Genes Dev. 13:1999;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
  • 24
    • 0035958556 scopus 로고    scopus 로고
    • Molecular analysis of kinetochore-microtubule attachment in budding yeast
    • He X., Rines D.R., Espelin C.W., Sorger P.K. Molecular analysis of kinetochore-microtubule attachment in budding yeast. Cell. 106:2001;195-206.
    • (2001) Cell , vol.106 , pp. 195-206
    • He, X.1    Rines, D.R.2    Espelin, C.W.3    Sorger, P.K.4
  • 25
    • 0036178929 scopus 로고    scopus 로고
    • Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation during mitosis by altering kinetochore-spindle pole connections
    • Elegant study revealing the role of Ipl1p in correcting monopolar kinetochore attachments; the authors postulate a model for Ipl1 regulation of chromosome biorientation in mitosis.
    • Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E., Stark M.J.R., Nasmyth K. Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation during mitosis by altering kinetochore-spindle pole connections. Cell. 108:2002;317-329 Elegant study revealing the role of Ipl1p in correcting monopolar kinetochore attachments; the authors postulate a model for Ipl1 regulation of chromosome biorientation in mitosis.
    • (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.R.7    Nasmyth, K.8
  • 26
    • 0028304675 scopus 로고
    • Type 1 protein phosphatase acts in opposition to Ipl1 protein kinase in regulating yeast chromosome segregation
    • Francisco L., Wang W., 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
  • 27
    • 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., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell. 102:2000;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    Grushcow, J.M.7    Brame, C.J.8    Caldwell, J.A.9    Hunt, D.F.10
  • 29
    • 0035923509 scopus 로고    scopus 로고
    • Yeast Dam1p has a role at the kinetochore in assembly of the mitotic spindle
    • Jones M.H., He X., Giddings T.H., Winey M. Yeast Dam1p has a role at the kinetochore in assembly of the mitotic spindle. Proc. Natl. Acad. Sci. U S A. 98:2001;13675-13680.
    • (2001) Proc. Natl. Acad. Sci. U S A , vol.98 , pp. 13675-13680
    • Jones, M.H.1    He, X.2    Giddings, T.H.3    Winey, M.4
  • 30
    • 0035956434 scopus 로고    scopus 로고
    • Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation
    • Kang J.S., Cheeseman I.M., Kallstrom G., Velmurugan S., Barnes G., Chan C.S. Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation. J. Cell. Biol. 155:2001;763-774.
    • (2001) J. Cell. Biol. , vol.155 , pp. 763-774
    • Kang, J.S.1    Cheeseman, I.M.2    Kallstrom, G.3    Velmurugan, S.4    Barnes, G.5    Chan, C.S.6
  • 33
    • 0037080488 scopus 로고    scopus 로고
    • The mitotic spindle is required for loading of the DASH complex onto the kinetochore
    • Identification and characterisation of the DASH complex and demonstration that Ipl1p regulates Dam1p phosphorylation.
    • Li Y., Bachant J., Alcasabas A.A., Wang Y., Qin J., Elledge S.J. The mitotic spindle is required for loading of the DASH complex onto the kinetochore. Genes Dev. 16:2002;183-197 Identification and characterisation of the DASH complex and demonstration that Ipl1p regulates Dam1p phosphorylation.
    • (2002) Genes Dev. , vol.16 , pp. 183-197
    • Li, Y.1    Bachant, J.2    Alcasabas, A.A.3    Wang, Y.4    Qin, J.5    Elledge, S.J.6
  • 34
    • 0041467803 scopus 로고    scopus 로고
    • Kinetochore protein interactions and their regulation by the Aurora kinase Ipl1p
    • Extensive characterisation of interactions between kinetochore components.
    • Shang C., Hazbun T.R., Cheeseman I.M., Aranda J., Fields S., Drubin D.G., Barnes G. Kinetochore protein interactions and their regulation by the Aurora kinase Ipl1p. Mol. Biol. Cell. 14:2003;3342-3355 Extensive characterisation of interactions between kinetochore components.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3342-3355
    • Shang, C.1    Hazbun, T.R.2    Cheeseman, I.M.3    Aranda, J.4    Fields, S.5    Drubin, D.G.6    Barnes, G.7
  • 35
    • 0035577762 scopus 로고    scopus 로고
    • The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint
    • Biggins S., 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
  • 36
    • 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., 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
  • 37
    • 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., 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
  • 38
    • 0036223874 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis
    • Leverson J.D., Huang H.K., Forsburg S.L., Hunter T. The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis. Mol. Biol. Cell. 13:2002;1132-1143.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1132-1143
    • Leverson, J.D.1    Huang, H.K.2    Forsburg, S.L.3    Hunter, T.4
  • 39
    • 0037380133 scopus 로고    scopus 로고
    • S. pombe Aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response
    • Petersen J., 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
  • 40
    • 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
    • The first evidence that in Drosophila Aurora B functions in chromosome congression and chromosome segregation.
    • Adams R.R., Maiato H., Earnshaw W.C., 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 The first evidence that in Drosophila Aurora B functions in chromosome congression and chromosome segregation.
    • (2001) J. Cell. Biol. , vol.153 , pp. 865-880
    • Adams, R.R.1    Maiato, H.2    Earnshaw, W.C.3    Carmena, M.4
  • 41
    • 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., 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
  • 42
    • 0032517860 scopus 로고    scopus 로고
    • AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos
    • Schumacher J.M., Golden A., Donovan P.J. AIR-2: An Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos. J. Cell. Biol. 143:1998;1635-1646.
    • (1998) J. Cell. Biol. , vol.143 , pp. 1635-1646
    • Schumacher, J.M.1    Golden, A.2    Donovan, P.J.3
  • 43
    • 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., 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
  • 44
    • 0037018844 scopus 로고    scopus 로고
    • Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
    • This paper describes anti-Xaurora B antibody injection experiments and live-cell imaging. Injection of antibodies against Aurora B blocks proper chromosome congression and abrogates the spindle checkpoint leading to premature exit from M-phase. Intriguingly, antibody injection also leads to stabilisation of astral microtubules in mitotic cells, but a loss of kinetochore/spindle microtubules. The authors speculate that Aurora B regulates the microtubule cytoskeleton by altering microtubule dynamics.
    • Kallio M.J., McCleland M.L., Stukenberg P.T., 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 This paper describes anti-Xaurora B antibody injection experiments and live-cell imaging. Injection of antibodies against Aurora B blocks proper chromosome congression and abrogates the spindle checkpoint leading to premature exit from M-phase. Intriguingly, antibody injection also leads to stabilisation of astral microtubules in mitotic cells, but a loss of kinetochore/spindle microtubules. The authors speculate that Aurora B regulates the microtubule cytoskeleton by altering microtubule dynamics.
    • (2002) Curr. Biol. , vol.12 , pp. 900-905
    • Kallio, M.J.1    Mccleland, M.L.2    Stukenberg, P.T.3    Gorbsky, G.J.4
  • 45
    • 0037018843 scopus 로고    scopus 로고
    • The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis
    • This paper describes the effects of overexpression of an Aurora B KR mutant in cells. By tracking single centromeres in live cells, Aurora B KR is shown to suppress the velocity of congressing chromosomes and to bias their normally saltatory behaviour to a more mono-directional one. Aurora B KR causes an increase in abnormal mitotic figures with prominent pole-to-pole microtubule bundles and numerous monopolar chromosomes clustered around the outside. Significantly, the authors find that kinetochore motors CENP-E and cytoplasmic dynein are depleted from kinetochores in Aurora B-KR-expressing cells.
    • Murata-Hori M., Wang Y.L. The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis. Curr. Biol. 12:2002;894-899 This paper describes the effects of overexpression of an Aurora B KR mutant in cells. By tracking single centromeres in live cells, Aurora B KR is shown to suppress the velocity of congressing chromosomes and to bias their normally saltatory behaviour to a more mono-directional one. Aurora B KR causes an increase in abnormal mitotic figures with prominent pole-to-pole microtubule bundles and numerous monopolar chromosomes clustered around the outside. Significantly, the authors find that kinetochore motors CENP-E and cytoplasmic dynein are depleted from kinetochores in Aurora B-KR-expressing cells.
    • (2002) Curr. Biol. , vol.12 , pp. 894-899
    • Murata-Hori, M.1    Wang, Y.L.2
  • 46
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • This is one of two papers to appear describing the effects of independently identified Aurora kinase inhibitors. The drug (ZM447439) used in this paper is a derivative of a compound that came out of a high-throughput screen for Aurora A inhibitors; as well as being a good inhibitor of Aurora kinases, it also inhibits other kinases in vitro. The ZM compound causes aneuploidy in cells lacking p53 because of a failure in cell division. Drug treatment of cells also leads to disrupted chromosome alignment, loss of centromere tension and segregation defects as well the loss of CENP-E, BubR1 and Mad2 from kinetochores. In these respects, ZM447439 treatment phenocopies Aurora B RNAi. Interestingly, ZM447439 also blocks BubRI phosphorylation, raising the intriguing possibility that Aurora B phosphorylates BubR1 directly, although ZM447439 could alter BubR1 modification indirectly by altering its localisation or inhibiting another kinase. BubRI RNAi was found to phenocopy Aurora B RNAi.
    • Ditchfield C., Johnson V.L., Tighe A., Ellston R., Haworth C., Johnson T., Mortlock A., Keen N., Taylor S.S. Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. J. Cell. Biol. 161:2003;267-280 This is one of two papers to appear describing the effects of independently identified Aurora kinase inhibitors. The drug (ZM447439) used in this paper is a derivative of a compound that came out of a high-throughput screen for Aurora A inhibitors; as well as being a good inhibitor of Aurora kinases, it also inhibits other kinases in vitro. The ZM compound causes aneuploidy in cells lacking p53 because of a failure in cell division. Drug treatment of cells also leads to disrupted chromosome alignment, loss of centromere tension and segregation defects as well the loss of CENP-E, BubR1 and Mad2 from kinetochores. In these respects, ZM447439 treatment phenocopies Aurora B RNAi. Interestingly, ZM447439 also blocks BubRI phosphorylation, raising the intriguing possibility that Aurora B phosphorylates BubR1 directly, although ZM447439 could alter BubR1 modification indirectly by altering its localisation or inhibiting another kinase. BubRI RNAi was found to phenocopy Aurora B RNAi.
    • (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    Mortlock, A.7    Keen, N.8    Taylor, S.S.9
  • 47
    • 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
    • note
    • ••], this largely phenocopies Aurora B RNAi. In a complex series of cell-cycle experiments, the authors show that Aurora B function is required around the time kinetochores are attaching to microtubules. Indeed the most significant result with regard to Aurora B's proposed function in mictotubule - kinetochore error correction comes from live-cell imaging of Hesperadin-treated PtK1 cells, which are seen to fail to correct mono-oriented chromosome attachments. Significantly, Hesperadin is shown in fixed cells to increase the frequency of syntelic attachments (where both kinetochores are attached to microtubules emanating from the same pole) in prometaphase. Analysis of monopolar chromosomes in monastrol-treated cells leads the authors to conclude that inhibition of Aurora B function may stabilise syntelics. Hesperadin treatment was shown to abrogate the spindle checkpoint induced by taxol and monastrol but not by nocodazole. BubR1 failed to be recruited to kinetochores in cells treated with Hesperadin and nocodazole.
    • (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
  • 49
    • 0038376119 scopus 로고    scopus 로고
    • Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension
    • •]), it is demonstrated that survivin-depleted cells arrest transiently in prometaphase and then exit mitosis without congressing or separating chromosomes. The authors show that survivin-depleted cells prematurely displace Mad2 and BubR1 from kinetochores. Survivin-depleted cells fail to arrest in taxol but arrest normally in nocodazole, implicating survivin in the BubR1-dependent arm of the spindle checkpoint that responds to lack of tension. In addition, the authors report a nice technical advance involving the introduction of RNAi-resistant survivin plasmids to complement cells depleted for survivin by RNAi, opening up myriad possibilities for the engineering of cell lines only expressing mutant forms of proteins.
    • •]), it is demonstrated that survivin-depleted cells arrest transiently in prometaphase and then exit mitosis without congressing or separating chromosomes. The authors show that survivin-depleted cells prematurely displace Mad2 and BubR1 from kinetochores. Survivin-depleted cells fail to arrest in taxol but arrest normally in nocodazole, implicating survivin in the BubR1-dependent arm of the spindle checkpoint that responds to lack of tension. In addition, the authors report a nice technical advance involving the introduction of RNAi-resistant survivin plasmids to complement cells depleted for survivin by RNAi, opening up myriad possibilities for the engineering of cell lines only expressing mutant forms of proteins.
    • (2003) EMBO J. , vol.22 , pp. 2934-2947
    • Lens, S.M.1    Wolthuis, R.M.2    Klompmaker, R.3    Kauw, J.4    Agami, R.5    Brummelkamp, T.6    Kops, G.7    Medema, R.H.8
  • 50
    • 0041941573 scopus 로고    scopus 로고
    • An Inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin
    • This paper describes the characterisation of a new protein, ICIS, from Xenopus extracts that resides in the inner centromere and interacts with MCAK, the microtubule-destabilising Kin I kinesin. Significantly, ICIS also co-precipitates Aurora B and INCENP. ICIS localisation on the inner centromere was found to depend on MCAK. In vitro ICIS has a stimulatory effect on MCAK activity. Addition of anti-ICIS antibodies to Xenopus spindle assembly reactions caused aberrant over-stabilised spindles. Using Immuno-EM, the authors show ICIS to be localized on the outer surfaces of kinetochores assembled from Xenopus extracts and argue that this may place ICIS-MCAK at a prime location for destabilising lateral or syntelic attachments.
    • Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J. An Inner centromere protein that stimulates the microtubule depolymerizing activity of a KinI kinesin. Dev. Cell. 5:2003;309-321 This paper describes the characterisation of a new protein, ICIS, from Xenopus extracts that resides in the inner centromere and interacts with MCAK, the microtubule-destabilising Kin I kinesin. Significantly, ICIS also co-precipitates Aurora B and INCENP. ICIS localisation on the inner centromere was found to depend on MCAK. In vitro ICIS has a stimulatory effect on MCAK activity. Addition of anti-ICIS antibodies to Xenopus spindle assembly reactions caused aberrant over-stabilised spindles. Using Immuno-EM, the authors show ICIS to be localized on the outer surfaces of kinetochores assembled from Xenopus extracts and argue that this may place ICIS-MCAK at a prime location for destabilising lateral or syntelic attachments.
    • (2003) Dev. Cell. , vol.5 , pp. 309-321
    • Ohi, R.1    Coughlin, M.L.2    Lane, W.S.3    Mitchison, T.J.4
  • 51
    • 0037415571 scopus 로고    scopus 로고
    • The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly
    • In this paper, Ipl1p is demonstrated to transfer the spindle midzone and, intriguingly, to follow the plus-ends of mictotubules as they depolymerise in late anaphase. An ipl1 mutant is shown to be defective in spindle disassembly in late anaphase and found to stabilise fragile spindles.
    • Buvelot S., Tatsutani S.Y., Vermaak D., Biggins S. The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly. J. Cell. Biol. 160:2003;329-339 In this paper, Ipl1p is demonstrated to transfer the spindle midzone and, intriguingly, to follow the plus-ends of mictotubules as they depolymerise in late anaphase. An ipl1 mutant is shown to be defective in spindle disassembly in late anaphase and found to stabilise fragile spindles.
    • (2003) J. Cell. Biol. , vol.160 , pp. 329-339
    • Buvelot, S.1    Tatsutani, S.Y.2    Vermaak, D.3    Biggins, S.4
  • 52
    • 0023580316 scopus 로고
    • The inner centromere protein (INCENP) antigens: Movement from inner centromere to midbody during mitosis
    • Cooke C.A., Heck M.M., Earnshaw W.C. The inner centromere protein (INCENP) antigens: movement from inner centromere to midbody during mitosis. J. Cell. Biol. 105:1987;2053-2067.
    • (1987) J. Cell. Biol. , vol.105 , pp. 2053-2067
    • Cooke, C.A.1    Heck, M.M.2    Earnshaw, W.C.3
  • 53
    • 0032498786 scopus 로고    scopus 로고
    • A dominant mutant of inner centromere protein (INCENP), a chromosomal protein, disrupts prometaphase congression and cytokinesis
    • Mackay A.M., Ainsztein A.M., Eckley D.M., Earnshaw W.C. A dominant mutant of inner centromere protein (INCENP), a chromosomal protein, disrupts prometaphase congression and cytokinesis. J. Cell. Biol. 140:1998;991-1002.
    • (1998) J. Cell. Biol. , vol.140 , pp. 991-1002
    • Mackay, A.M.1    Ainsztein, A.M.2    Eckley, D.M.3    Earnshaw, W.C.4
  • 54
    • 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., 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
  • 55
    • 0035810919 scopus 로고    scopus 로고
    • INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis
    • Wheatley S.P., Carvalho A., Vagnarelli P., Earnshaw W.C. INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis. Curr. Biol. 11:2001;886-890.
    • (2001) Curr. Biol. , vol.11 , pp. 886-890
    • Wheatley, S.P.1    Carvalho, A.2    Vagnarelli, P.3    Earnshaw, W.C.4
  • 56
    • 0036223382 scopus 로고    scopus 로고
    • Probing the dynamics and functions of aurora B kinase in living cells during mitosis and cytokinesis
    • Aurora B dynamics are followed over time in live cells, showing that Aurora B leaves centromeres at anaphase onset and moves onto midzone microtubules. Inhibiting CDK1 deactivation by microinjection of mRNA encoding cyclin B Δ90 blocks loss of Aurora B from centromeres, despite the onset of anaphase, ultimately leading to a failure in cytokinesis; however, this effect was not found in cells treated with a CDK1 inhibitor.
    • Murata-Hori M., Tatsuka M., Wang Y.L. Probing the dynamics and functions of aurora B kinase in living cells during mitosis and cytokinesis. Mol. Biol. Cell. 13:2002;1099-1108 Aurora B dynamics are followed over time in live cells, showing that Aurora B leaves centromeres at anaphase onset and moves onto midzone microtubules. Inhibiting CDK1 deactivation by microinjection of mRNA encoding cyclin B Δ90 blocks loss of Aurora B from centromeres, despite the onset of anaphase, ultimately leading to a failure in cytokinesis; however, this effect was not found in cells treated with a CDK1 inhibitor.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 1099-1108
    • Murata-Hori, M.1    Tatsuka, M.2    Wang, Y.L.3
  • 57
    • 0037078332 scopus 로고    scopus 로고
    • Both midzone and astral microtubules are involved in the delivery of cytokinesis signals: Insights from the mobility of aurora B
    • This study explores Aurora B dynamics using FRAP, showing that its turnover changes from a relatively fast rate during metaphase to a slow rate during anaphase. Bleaching experiments suggest that two populations of Aurora B exist, with cortical Aurora B localisation at the cleavage furrow derived from a different population from centromere-derived Aurora B, which ends up on midzone microtubules.
    • Murata-Hori M., Wang Y.I. Both midzone and astral microtubules are involved in the delivery of cytokinesis signals: insights from the mobility of aurora B. J. Cell. Biol. 159:2002;45-54 This study explores Aurora B dynamics using FRAP, showing that its turnover changes from a relatively fast rate during metaphase to a slow rate during anaphase. Bleaching experiments suggest that two populations of Aurora B exist, with cortical Aurora B localisation at the cleavage furrow derived from a different population from centromere-derived Aurora B, which ends up on midzone microtubules.
    • (2002) J. Cell. Biol. , vol.159 , pp. 45-54
    • Murata-Hori, M.1    Wang, Y.I.2
  • 58
    • 0033602489 scopus 로고    scopus 로고
    • Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis
    • Fraser A.G., James C., Evan G.I., Hengartner M.O. Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis. Curr. Biol. 9:1999;292-301.
    • (1999) Curr. Biol. , vol.9 , pp. 292-301
    • Fraser, A.G.1    James, C.2    Evan, G.I.3    Hengartner, M.O.4
  • 59
    • 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., 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
  • 60
    • 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., 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
  • 61
    • 0036007115 scopus 로고    scopus 로고
    • Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity
    • Mishima M., Kaitna S., Glotzer M. Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity. Dev. Cell. 2:2002;41-54.
    • (2002) Dev. Cell. , vol.2 , pp. 41-54
    • Mishima, M.1    Kaitna, S.2    Glotzer, M.3
  • 62
    • 0037387766 scopus 로고    scopus 로고
    • Phosphorylation by Aurora B converts MgcRacGAP to a RhoGAP during cytokinesis
    • This study shows that MgcRacGAP (the orthologue of CYK-4), which is part of the midzone microtubule-associated complex, is phosphorylated by Aurora B. Significantly, Aurora B phosphorylation of mgcRacGAP converts its activity from a GTPase-activating protein specific for Rac to one specific for Rho in vitro. An alanine mutation at a single serine residue, identified as a target for Aurora B, blocks cytokinesis, leading to polyploidy.
    • Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A., Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr. Phosphorylation by Aurora B converts MgcRacGAP to a RhoGAP during cytokinesis. Dev. Cell. 4:2003;549-560 This study shows that MgcRacGAP (the orthologue of CYK-4), which is part of the midzone microtubule-associated complex, is phosphorylated by Aurora B. Significantly, Aurora B phosphorylation of mgcRacGAP converts its activity from a GTPase-activating protein specific for Rac to one specific for Rho in vitro. An alanine mutation at a single serine residue, identified as a target for Aurora B, blocks cytokinesis, leading to polyploidy.
    • (2003) Dev. Cell. , vol.4 , pp. 549-560
    • Minoshima, Y.1    Kawashima, T.2    Hirose, K.3    Tonozuka, Y.4    Kawajiri, A.5    Bao, Y.C.6    Deng, X.7    Tatsuka, M.8    Narumiya, S.9    May, W.S.Jr.10
  • 64
    • 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.i., 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.I.6    Inagaki, M.7
  • 67
    • 0042679490 scopus 로고    scopus 로고
    • Determining the position of the cell division plane
    • This study probes the role of microtubule dynamics in the positioning of cell division plane.
    • Canman J.C., Cameron L.A., Maddox P.S., Straight A., Tirnauer J.S., Mitchison T.J., Fang G., Kapoor T.M., Salmon E.D. Determining the position of the cell division plane. Nature. 424:2003;1074-1078 This study probes the role of microtubule dynamics in the positioning of cell division plane.
    • (2003) Nature , vol.424 , pp. 1074-1078
    • Canman, J.C.1    Cameron, L.A.2    Maddox, P.S.3    Straight, A.4    Tirnauer, J.S.5    Mitchison, T.J.6    Fang, G.7    Kapoor, T.M.8    Salmon, E.D.9
  • 68
    • 0035945340 scopus 로고    scopus 로고
    • CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis
    • Zeitlin S.G., Shelby R.D., Sullivan K.F. CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis. J. Cell. Biol. 155:2001;1147-1157.
    • (2001) J. Cell. Biol. , vol.155 , pp. 1147-1157
    • Zeitlin, S.G.1    Shelby, R.D.2    Sullivan, K.F.3
  • 72
    • 0036153807 scopus 로고    scopus 로고
    • ISWI remodeling complexes in Xenopus egg extracts: Identification as major chromosomal components that are regulated by INCENP-Aurora B
    • MacCallum D.E., Losada A., Kobayashi R., Hirano T. ISWI remodeling complexes in Xenopus egg extracts: identification as major chromosomal components that are regulated by INCENP-Aurora B. Mol. Biol. Cell. 13:2002;25-39.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 25-39
    • Maccallum, D.E.1    Losada, A.2    Kobayashi, R.3    Hirano, T.4
  • 73
    • 0037349338 scopus 로고    scopus 로고
    • The making of the mitotic chromosome. Modern insights into classical questions
    • Swedlow J.R., 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
  • 74
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei Y., Yu L., Bowen J., Gorovsky M.A., Allis C.D. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell. 97:1999;99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 75
    • 0037087623 scopus 로고    scopus 로고
    • C. elegans condensin promotes mitotic chromosome architecture, centromere organization, and sister chromatid segregation during mitosis and meiosis
    • Hagstrom K.A., Holmes V.F., Cozzarelli N.R., Meyer B.J. C. elegans condensin promotes mitotic chromosome architecture, centromere organization, and sister chromatid segregation during mitosis and meiosis. Genes Dev. 16:2002;729-742.
    • (2002) Genes Dev. , vol.16 , pp. 729-742
    • Hagstrom, K.A.1    Holmes, V.F.2    Cozzarelli, N.R.3    Meyer, B.J.4
  • 76
    • 0037018157 scopus 로고    scopus 로고
    • In vivo dissection of the chromosome condensation machinery: Reversibility of condensation distinguishes contributions of condensin and cohesin
    • Lavoie B.D., Hogan E., Koshland D. In vivo dissection of the chromosome condensation machinery: reversibility of condensation distinguishes contributions of condensin and cohesin. J. Cell. Biol. 156:2002;805-815.
    • (2002) J. Cell. Biol. , vol.156 , pp. 805-815
    • Lavoie, B.D.1    Hogan, E.2    Koshland, D.3
  • 77
    • 0036896143 scopus 로고    scopus 로고
    • Cohesin release is required for sister chromatid resolution, but not for condensin-mediated compaction, at the onset of mitosis
    • This paper describes the effects of depletion of Aurora B and/or Polo from Xenopus extracts. Depletion of both kinases leads to normal condensation and condensin loading but failure in the prophase loss of cohesin and subsequently a failure to resolve sisters.
    • Losada A., Hirano M., 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 This paper describes the effects of depletion of Aurora B and/or Polo from Xenopus extracts. Depletion of both kinases leads to normal condensation and condensin loading but failure in the prophase loss of cohesin and subsequently a failure to resolve sisters.
    • (2002) Genes Dev. , vol.16 , pp. 3004-3016
    • Losada, A.1    Hirano, M.2    Hirano, T.3
  • 78
    • 0037092044 scopus 로고    scopus 로고
    • The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis
    • This study shows that disruption of C. elegans Aurora B/AIR-2 leads to a failure to release of REC-8 cohesin from meiotic chromosomes, resulting in disrupted chromosome segregation. REC-8 is reported to be a substrate of Aurora B. Depletion of GLC7 phosphatases leads to delocalisation of Aurora B, premature release of REC-8 and premature loss of sister cohesion.
    • Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R. The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis. J. Cell. Biol. 157:2002;219-229 This study shows that disruption of C. elegans Aurora B/AIR-2 leads to a failure to release of REC-8 cohesin from meiotic chromosomes, resulting in disrupted chromosome segregation. REC-8 is reported to be a substrate of Aurora B. Depletion of GLC7 phosphatases leads to delocalisation of Aurora B, premature release of REC-8 and premature loss of sister cohesion.
    • (2002) J. Cell. Biol. , vol.157 , pp. 219-229
    • Rogers, E.1    Bishop, J.D.2    Waddle, J.A.3    Schumacher, J.M.4    Lin, R.5
  • 79
    • 0032213515 scopus 로고    scopus 로고
    • Multinuclearity and increased ploidy caused by overexpression of the aurora- and Ipl1-like midbody-associated protein mitotic kinase in human cancer cells
    • Tatsuka M., Katayama H., Ota T., Tanaka T., Odashima S., Suzuki F., Terada Y. Multinuclearity and increased ploidy caused by overexpression of the aurora- and Ipl1-like midbody-associated protein mitotic kinase in human cancer cells. Cancer Res. 58:1998;4811-4816.
    • (1998) Cancer Res. , vol.58 , pp. 4811-4816
    • Tatsuka, M.1    Katayama, H.2    Ota, T.3    Tanaka, T.4    Odashima, S.5    Suzuki, F.6    Terada, Y.7
  • 80
    • 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., Schumacher J.M. Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B kinase stimulates Aurora B kinase activity. J. Biol. Chem. 277:2002;27577-27580.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27577-27580
    • Bishop, J.D.1    Schumacher, J.M.2
  • 81
    • 0041968963 scopus 로고    scopus 로고
    • Exploring the functional interactions between Aurora B, INCENP, and Survivin in mitosis
    • Honda R., Korner R., Nigg E.A. Exploring the functional interactions between Aurora B, INCENP, and Survivin in mitosis. Mol. Biol. Cell. 14:2003;3325-3341.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3325-3341
    • Honda, R.1    Korner, R.2    Nigg, E.A.3
  • 84
    • 0037447055 scopus 로고    scopus 로고
    • Cyclin B destruction triggers changes in kinetochore behavior essential for successful anaphase
    • This paper describes experiments in Drosophila embryos engineered to express a non-degradable cyclin B. During arrest, sister chromosomes disjoin but display unusual oscillatory behaviour, accumulate merotelic attachments, congress to a pseudo-prometaphase state and reacquire checkpoint proteins on their kinetochores. This was phenocopied using the double-parked mutant, which enters anaphase with unreplicated and therefore unpaired chromosomes. Significantly, Aurora B/INCENP release from centromeres is blocked by expression of non-degradable cyclin B and conversely is lost prematurely in a cyclin B mutant line.
    • Parry D.H., Hickson G.R., O'Farrell P.H. Cyclin B destruction triggers changes in kinetochore behavior essential for successful anaphase. Curr. Biol. 13:2003;647-653 This paper describes experiments in Drosophila embryos engineered to express a non-degradable cyclin B. During arrest, sister chromosomes disjoin but display unusual oscillatory behaviour, accumulate merotelic attachments, congress to a pseudo-prometaphase state and reacquire checkpoint proteins on their kinetochores. This was phenocopied using the double-parked mutant, which enters anaphase with unreplicated and therefore unpaired chromosomes. Significantly, Aurora B/INCENP release from centromeres is blocked by expression of non-degradable cyclin B and conversely is lost prematurely in a cyclin B mutant line.
    • (2003) Curr. Biol. , vol.13 , pp. 647-653
    • Parry, D.H.1    Hickson, G.R.2    O'farrell, P.H.3
  • 86
    • 12244296163 scopus 로고    scopus 로고
    • Depletion of drad21/scc1 in Drosophila cells leads to instability of the cohesin complex and disruption of mitotic progression
    • Vass S., Cotterill S., Valdeolmillos A.M., Barbero J.L., Lin E., Warren W.D., Heck M.M. Depletion of drad21/scc1 in Drosophila cells leads to instability of the cohesin complex and disruption of mitotic progression. Curr. Biol. 13:2003;208-218.
    • (2003) Curr. Biol. , vol.13 , pp. 208-218
    • Vass, S.1    Cotterill, S.2    Valdeolmillos, A.M.3    Barbero, J.L.4    Lin, E.5    Warren, W.D.6    Heck, M.M.7
  • 87
    • 0041440100 scopus 로고    scopus 로고
    • Condensin is required for nonhistone protein assembly and structural integrity of vertebrate mitotic chromosomes
    • Hudson D.F., Vagnarelli P., Gassmann R., Earnshaw W.C. Condensin is required for nonhistone protein assembly and structural integrity of vertebrate mitotic chromosomes. Dev. Cell. 5:2003;323-336.
    • (2003) Dev. Cell. , vol.5 , pp. 323-336
    • Hudson, D.F.1    Vagnarelli, P.2    Gassmann, R.3    Earnshaw, W.C.4
  • 88
    • 0032576619 scopus 로고    scopus 로고
    • INCENP centromere and spindle targeting: Identification of essential conserved motifs and involvement of heterochromatin protein HP1
    • Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C. INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. J. Cell. Biol. 143:1998;1763-1774.
    • (1998) J. Cell. Biol. , vol.143 , pp. 1763-1774
    • Ainsztein, A.M.1    Kandels-Lewis, S.E.2    Mackay, A.M.3    Earnshaw, W.C.4
  • 89
    • 0037390327 scopus 로고    scopus 로고
    • Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development
    • Rangasamy D., Berven L., Ridgway P., Tremethick D.J. Pericentric heterochromatin becomes enriched with H2A.Z during early mammalian development. EMBO J. 22:2003;1599-1607.
    • (2003) EMBO J. , vol.22 , pp. 1599-1607
    • Rangasamy, D.1    Berven, L.2    Ridgway, P.3    Tremethick, D.J.4
  • 91
    • 0037244295 scopus 로고    scopus 로고
    • Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle
    • This paper demonstrates for the first time the kinetochore localisation of PP1 in live and fixed cells. It shows by FRAP analysis that PP1 turnover is highly dynamic.
    • Trinkle-Mulcahy L., Andrews P.D., Wickramasinghe S., Sleeman J., Prescott A., Lam Y.W., Lyon C., Swedlow J.R., Lamond A.I. Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle. Mol. Biol. Cell. 14:2003;107-117 This paper demonstrates for the first time the kinetochore localisation of PP1 in live and fixed cells. It shows by FRAP analysis that PP1 turnover is highly dynamic.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 107-117
    • Trinkle-Mulcahy, L.1    Andrews, P.D.2    Wickramasinghe, S.3    Sleeman, J.4    Prescott, A.5    Lam, Y.W.6    Lyon, C.7    Swedlow, J.R.8    Lamond, A.I.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.