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Provides one of the first insights into the link between Aurora kinases and carcinogenesis.
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Berdnik, D. & Knoblich, J. A. Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis. Curr. Biol. 12, 640–647 (2002).
This describes a role for Aurora A in asymmetric cell division and examines the dynamics of Aurora-A association with centrosomes.
Wittmann, T., Wilm, M., Karsenti, E. & Vernos, I. TPX2, a novel Xenopus MAP involved in spindle pole organization. J. Cell Biol. 149, 1405–1418 (2000).
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Giet, R. & Prigent, C. The non-catalytic domain of the Xenopus laevis aurora A kinase localises the protein to the centrosome. J. Cell Sci. 114, 2095–2104 (2001).
Giet, R. et al. Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules. J. Cell Biol. 156, 437–451 (2002).
RNAi analysis confirms a role for Aurora A in centrosome maturation and separation.
Kufer, T. A. et al. Human TPX2 is required for targeting Aurora-A kinase to the spindle. J. Cell Biol. 158, 617–623 (2002).
Hannak, E., Kirkham, M., Hyman, A. A. & Oegema, K. Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans. J. Cell Biol. 155, 1109–1116 (2001).
Giet, R., Uzbekov, R., Cubizolles, F., Le Guellec, K. & Prigent, C. The Xenopus laevis aurora-related protein kinase pEg2 associates with and phosphorylates the kinesin-related protein XlEg5. J. Biol. Chem. 274, 15005–15013 (1999).
Tsai, M. Y. et al. A Ran signalling pathway mediated by the mitotic kinase Aurora A in spindle assembly. Nature Cell Biol. 5, 242–248 (2003).
This study shows that TPX2 activates Aurora-A kinase, and proposes that Aurora A might be an important downstream target of Ran–GTP in promoting mitotic spindle assembly.
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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, 691–697 (2003).
This study shows that TPX2 activates Aurora-A kinase in part by blocking the inactivation of the kinase by protein phosphatase 1.
Andresson, T. & Ruderman, J. V. The kinase Eg2 is a component of the Xenopus oocyte progesterone-activated signaling pathway. EMBO J. 17, 5627–5637 (1998).
Mendez, R. et al. Phosphorylation of CPE binding factor by Eg2 regulates translation of c-mos mRNA. Nature 404, 302–307 (2000).
This describes the involvement of Aurora A in cell-cycle regulation by regulating poly(A)-dependent translation.
Frank-Vaillant, M. et al. Progesterone regulates the accumulation and the activation of Eg2 kinase in Xenopus oocytes. J. Cell Sci. 113, 1127–1138 (2000).
Maton, G. et al. Cdc2–Cyclin B triggers H3 kinase activation of Aurora-A in Xenopus oocytes. J. Biol. Chem. 278, 21439–21449 (2003).
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, 1635–1646 (1998).
Castro, A., Mandart, E., Lorca, T. & Galas, S. Involvement of Aurora A kinase during meiosis I–II transition in Xenopus oocytes. J. Biol. Chem. 278, 2236–2241 (2003).
Littlepage, L. E. et al. Identification of phosphorylated residues that affect the activity of the mitotic kinase Aurora-A. Proc. Natl Acad. Sci. USA 99, 15440–15445 (2002).
Systematic analysis of the residues that are relevant for regulation of Aurora-A kinase.
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, 4906–4916 (2000).
Cheeseman, I. M. et al. Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p. Cell 111, 163–172 (2002).
This is the most thorough study yet of the protein targets of the Aurora kinase Ipl1.
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, 4731–4740 (1994).
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Castro, A. et al. APC/Fizzy-Related targets Aurora-A kinase for proteolysis. EMBO Rep. 3, 457–462 (2002).
Castro, A. et al. The D-Box-activating domain (DAD) is a new proteolysis signal that stimulates the silent D-Box sequence of Aurora-A. EMBO Rep. 3, 1209–1214 (2002).
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References 46 and 48 do a good job of dissecting the complexities of Aurora-A regulation by the APC/C.
Kiat, L. S., Hui, K. M. & Gopalan, G. Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase. J. Biol. Chem. 277, 45558–45565 (2002).
Terada, Y. et al. AIM-1: a mammalian midbody-associated protein required for cytokinesis. EMBO J. 17, 667–676 (1998).
One of the first reports showing the requirement of Aurora B for cytokinesis.
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, 865–880 (2001).
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, 1099–1108 (2002).
Examines the dynamic behaviour of Aurora-B kinase in vivo using green-fluorescent-protein-labelled protein.
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Nicklas, R. B., Wards, S. C. & Gorbsky, G. J. Kinetochore chemistry is sensitive to tension and may link mitotic forces for a cell cycle checkpoint. J. Cell Biol. 130, 929–939 (1995).
Tanaka, T. U. et al. Evidence that the Ipl1–Sli15 (Aurora kinase–INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections. Cell 108, 317–329 (2002).
This paper was the first to propose that Ipl1 might be involved in the resolution of syntelic chromsome attachments.
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, 900–905 (2002).
Antibody injection is used to identify some of the many functions of Aurora B in mammalian cells.
Ditchfield, C. et al. Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2 and Cenp-E to kinetochores. J. Cell Biol. 161, 267–280 (2003).
This description of a small-molecule inhibitor of Aurora B identifies a role for the kinase in the spindle-assembly checkpoint when the checkpoint is activated in the presence of microtubules by altering tension within the spindle.
Hauf, S. et al. The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint. J. Cell Biol. 161, 281–294 (2003).
This description of a second small-molecule inhibitor of Aurora B provides the best evidence to date that the kinase is involved in the resolution of syntelic chromosomal attachments during prometaphase.
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Honda, R., Korner, R. & Nigg, E. A. Exploring the functional interactions between Aurora B, INCENP, and survivin in mitosis. Mol. Biol. Cell 14, 3325–3341 (2003).
A thorough study of the regulation of Aurora-B kinase activity by INCENP and survivin.
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, 1147–1157 (2001).
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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, 669–681 (2001).
Crosio, C. et al. Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases. Mol. Cell. Biol. 22, 874–885 (2002).
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Goto, H., Yasui, Y., Nigg, E. A. & Inagaki, M. Aurora-B phosphorylates Histone H3 at serine28 with regard to the mitotic chromosome condensation. Genes Cells 7, 11–17 (2002).
Giet, R. & Prigent, C. The Xenopus laevis aurora/Ip11p-related kinase pEg2 participates in the stability of the bipolar mitotic spindle. Exp. Cell Res. 258, 145–151 (2000).
Hirano, T. The ABCs of SMC proteins: two-armed ATPases for chromosome condensation, cohesion, and repair. Genes Dev. 16, 399–414 (2002).
Petersen, J. & Hagan, I. M. S. pombe Aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response. Curr. Biol. 13, 590–597 (2003).
This study uses yeast genetics to show a role for Aurora B and its associated protein survivin in the spindle-assembly checkpoint.
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, 798–812 (2002).
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, 729–742 (2002).
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, 219–229 (2002).
This provides important insights into the role of Aurora B in chromosome segregation in meiosis.
Sonoda, E. et al. Scc1/Rad21/Mcd1 is required for sister chromatid cohesion and kinetochore function in vertebrate cells. Dev. Cell 1, 759–770 (2001).
Mackay, A. M., Ainsztein, A., 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, 991–1002 (1998).
Adams, R. R. et al. INCENP binds the aurora-related kinase AIRK2 and is required to target it to chromosomes, the central spindle and cleavage furrow. Curr. Biol 10, 1075–1078 (2000).
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, 1172–1181 (2000).
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, 1162–1171 (2000).
Murata-Hori, M. et al. Myosin II regulatory light chain as a novel substrate for AIM-1, an aurora/Ipl1p-related kinase from rat. J. Biochem. (Tokyo) 128, 903–907 (2000).
Goto, H. et al. Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J. Biol. Chem. 278, 8526–8530 (2003).
Kawajiri, A. et al. 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, 1489–1500 (2003).
Jantsch-Plunger, V. et al. CYK-4: A Rho family GTPase activating protein (GAP) required for central spindle formation and cytokinesis. J. Cell Biol. 149, 1391–1404 (2000).
Minoshima, Y., et al. Phosphorylation by Aurora B converts MgcRacGAP to a RhoGAP during cytokinesis. Dev. Cell 4, 549–560 (2003).
An elegant study that identifies a new substrate for Aurora B and shows how the kinase might participate in the regulation of cytokinesis.
Kishi, K., Sasaki, T., Kuroda, S., Itoh, T. & Takai, Y. Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J. Cell Biol. 120, 1187–1195 (1993).
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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, 3118–3129 (2001).
Carvalho, A., Carmena, M., Sambade, C., Earnshaw, W. C. & Wheatley, S. P. Survivin is required for stable checkpoint activation in taxol-treated HeLa cells. J. Cell Sci. 116, 2987–2998 (2003).
Lens, S. M. A. et al. Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension. EMBO J. 22, 2934–2947 (2003).
References 93 and 94 use RNAi technology to show that survivin is required for the spindle-assembly checkpoint in the presence of microtubules, and for BubR1 targeting to the kinetochore.
Sugiyama, K. et al. Aurora-B associated protein phosphatases as negative regulators of kinase activation. Oncogene 21, 3103–3111 (2002).
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, 886–890 (2001).
Bolton, M. A. et al. Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation. Mol. Biol. Cell 13, 3064–3077 (2002).
A thorough study of the regulation of Aurora-B kinase activity by INCENP and survivin.
Wheatley, S. P., Kandels-Lewis, S. E., Adams, R. R., Ainsztein, A. M. & Earnshaw, W. C. INCENP binds directly to tubulin and requires dynamic microtubules to target to the cleavage furrow. Exp. Cell. Res. 262, 122–127 (2001).
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, 1763–1774 (1998).
Terada, Y., Katayama, H., Tatsuka, M. & Kuriyama, R. AIM-1 regulates onset of cytokinesis by targeting INCENP to midzone and midbody. Mol. Biol. Cell 11S, 343a (2000).
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, 27577–27580 (2002).
Provided a clear demonstration that INCENP phosphorylation by Aurora B is part of a feedback loop that stimulates kinase activity.
Deveraux, Q. L. & Reed, J. C. IAP family proteins — suppressors of apoptosis. Genes Dev. 13, 239–252 (1999).
Uren, A. G. et al. Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype. Curr. Biol. 10, 1319–1328 (2000).
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Morishita, J. et al. Bir1/Cut17 moving from chromosome to spindle upon the loss of cohesion is required for condensation, spindle elongation and repair. Genes Cells 6, 743–763 (2001).
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Meraldi, P., Honda, R. & Nigg, E. A. Aurora-A overexpression reveals tetraploidization as a major route to centrosome amplification in p53−/− cells. EMBO J. 21, 483–492 (2002).
Presents data indicating that centrosome amplification in response to Aurora kinase overexpression arises as a result of failures in cytokinesis.
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