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Volumn 14, Issue 1, 2004, Pages 29-36

Aurora kinases link chromosome segregation and cell division to cancer susceptibility

Author keywords

[No Author keywords available]

Indexed keywords

AURORA A KINASE; AURORA B KINASE; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0842281498     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gde.2003.11.006     Document Type: Review
Times cited : (294)

References (62)
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    • On the role of aurora-A in centrosome function
    • A broad review on the role of Aurora A in centrosome function and spindle assembly as well as its contribution to oncogenesis.
    • Dutertre S., Descamps S., Prigent C. On the role of aurora-A in centrosome function. Oncogene. 21:2002;6175-6183 A broad review on the role of Aurora A in centrosome function and spindle assembly as well as its contribution to oncogenesis.
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    • Chromosome dynamics: New light on aurora B kinase function
    • An excellent, concise review on the multiple functions of Aurora B.
    • Shannon K.B., Salmon E.D. Chromosome dynamics: New light on aurora B kinase function. Curr Biol. 12:2002;R458-R460 An excellent, concise review on the multiple functions of Aurora B.
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    • Identification of phosphorylated residues that affect the activity of the mitotic kinase Aurora-A
    • ••]). Most interestingly, mutation of a serine residue within this motif (serine 53 in Xenopus) to aspartic acid blocks degradation, suggesting that dephosphorylation of this site may contribute to control the timing of Aurora A destruction.
    • ••]). Most interestingly, mutation of a serine residue within this motif (serine 53 in Xenopus) to aspartic acid blocks degradation, suggesting that dephosphorylation of this site may contribute to control the timing of Aurora A destruction.
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    • Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
    • ••]). It also shows that the mutation of a conserved lysine (169) to arginine, a mutation frequently used to generate 'inactive' versions of kinases, still retains ∼10% of wild-type activity.
    • ••]). It also shows that the mutation of a conserved lysine (169) to arginine, a mutation frequently used to generate 'inactive' versions of kinases, still retains ∼10% of wild-type activity.
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    • A novel mechanism for activation of the protein kinase aurora a
    • An unbiased search for activators of Aurora A in Xenopus egg extracts led to the identification of TPX2 as a potent activator of Aurora A kinase. Interestingly, in this study MTs were not required for kinase activation. The data further indicate that kinase activation by TPX2 results from the stimulation of autophosphorylation in the regulatory T-loop of the kinase.
    • 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 An unbiased search for activators of Aurora A in Xenopus egg extracts led to the identification of TPX2 as a potent activator of Aurora A kinase. Interestingly, in this study MTs were not required for kinase activation. The data further indicate that kinase activation by TPX2 results from the stimulation of autophosphorylation in the regulatory T-loop of the kinase.
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    • Eyers, P.A.1    Erikson, E.2    Chen, L.G.3    Maller, J.L.4
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    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • This thorough study elucidates the mechanism of Aurora A activation by TPX2. Combining biochemical approaches with crystallographic studies, the authors provide evidence that TPX2 binding and phosphorylation of a conserved residue in the activation domain act synergistically to lock the kinase in an active conformation.
    • Bayliss R., Sardon T., Vernos I., Conti E. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol Cell. 12:2003;851-862 This thorough study elucidates the mechanism of Aurora A activation by TPX2. Combining biochemical approaches with crystallographic studies, the authors provide evidence that TPX2 binding and phosphorylation of a conserved residue in the activation domain act synergistically to lock the kinase in an active conformation.
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    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4
  • 14
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    • 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
    • •]). In addition, overexpression of Aurora A was shown to transform NIH 3T3 cells.
    • •]). In addition, overexpression of Aurora A was shown to transform NIH 3T3 cells.
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    • Littlepage, L.E.1    Ruderman, J.V.2
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    • 0037160088 scopus 로고    scopus 로고
    • Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase
    • The authors have exploited the lethal phenotype associated with overexpression of Aurora A in yeast to isolate a ubiquitously expressed nuclear protein, termed AIP (Aurora A kinase interacting protein). They report that AIP down-regulates Aurora A in a proteasome-dependent manner.
    • 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. 277:2002;45558-45565 The authors have exploited the lethal phenotype associated with overexpression of Aurora A in yeast to isolate a ubiquitously expressed nuclear protein, termed AIP (Aurora A kinase interacting protein). They report that AIP down-regulates Aurora A in a proteasome-dependent manner.
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    • Kiat, L.S.1    Hui, K.M.2    Gopalan, G.3
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    • 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
    • With Csc-1, a fourth essential subunit of the Aurora B kinase complex is identified in C. elegans. However, this subunit is not conserved in vertebrates. One plausible explanation of the data is that the C. elegans Csc-1 functionally substitutes for the N-terminal coiled-coil domain of vertebrate INCENP.
    • 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 With Csc-1, a fourth essential subunit of the Aurora B kinase complex is identified in C. elegans. However, this subunit is not conserved in vertebrates. One plausible explanation of the data is that the C. elegans Csc-1 functionally substitutes for the N-terminal coiled-coil domain of vertebrate INCENP.
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    • INCENP is required for proper targeting of Survivin to the centromeres and the anaphase spindle during mitosis
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    • Functional cooperation of Dam1, Ipl1, and the inner centromere protein (INCENP)-related protein Sli15 during chromosome segregation
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    • Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B Kinase stimulates Aurora B kinase activity
    • •]).
    • •]).
    • (2002) J Biol Chem , vol.277 , pp. 27577-27580
    • Bishop, J.D.1    Schumacher, J.M.2
  • 23
    • 0036732808 scopus 로고    scopus 로고
    • Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
    • Using Xenopus egg extracts, the authors performed a careful study on the role of survivin in the activation of Aurora B. They report that virtually all survivin exists in a complex with Aurora B and that kinase activity is regulated by both survivin and cell-cycle-dependent phosphorylation.
    • Bolton M.A., Lan W., Powers S.E., McCleland M.L., Kuang J., Stukenberg P.T. 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. 13:2002;3064-3077 Using Xenopus egg extracts, the authors performed a careful study on the role of survivin in the activation of Aurora B. They report that virtually all survivin exists in a complex with Aurora B and that kinase activity is regulated by both survivin and cell-cycle-dependent phosphorylation.
    • (2002) Mol Biol Cell , vol.13 , pp. 3064-3077
    • Bolton, M.A.1    Lan, W.2    Powers, S.E.3    Mccleland, M.L.4    Kuang, J.5    Stukenberg, P.T.6
  • 25
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    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
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  • 26
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    • 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.
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    • Giet, R.1    Glover, D.M.2
  • 27
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    • Mitotic phosphorylation of histone H3: Spatio-temporal regulation by mammalian Aurora kinases
    • This study correlates the localization of Aurora A and B in mammalian cells with histone H3 phosphorylation. Both kinases are also shown to phosphorylate histone H3 and to bind to the histone H3 tail in vitro.
    • Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S., Allis C.D., Sassone-Corsi P. Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases. Mol Cell Biol. 22:2002;874-885 This study correlates the localization of Aurora A and B in mammalian cells with histone H3 phosphorylation. Both kinases are also shown to phosphorylate histone H3 and to bind to the histone H3 tail in vitro.
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    • Crosio, C.1    Fimia, G.M.2    Loury, R.3    Kimura, M.4    Okano, Y.5    Zhou, H.6    Sen, S.7    Allis, C.D.8    Sassone-Corsi, P.9
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    • CENP-A is phosphorylated by Aurora B kinase and plays an unexpected role in completion of cytokinesis
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    • Zeitlin, S.G.1    Shelby, R.D.2    Sullivan, K.F.3
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    • Increased mitotic phosphorylation of histone H3 attributable to AIM-1/Aurora-B overexpression contributes to chromosome number instability
    • Overexpression of Aurora B in hamster cells was shown to cause increased histone H3 phosphorylation and concomitant induction of lagging chromosomes. As similar phenotypes could be observed upon expression of a mutant histone H3 (S10E) that mimics phosphorylation at serine 10, it is proposed that deregulated histone H3 phosphorylation could contribute to chromosome mis-segregation in tumor cells that overexpress Aurora kinases.
    • Ota T., Suto S., Katayama H., Han Z.B., Suzuki F., Maeda M., Tanino M., Terada Y., 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 Overexpression of Aurora B in hamster cells was shown to cause increased histone H3 phosphorylation and concomitant induction of lagging chromosomes. As similar phenotypes could be observed upon expression of a mutant histone H3 (S10E) that mimics phosphorylation at serine 10, it is proposed that deregulated histone H3 phosphorylation could contribute to chromosome mis-segregation in tumor cells that overexpress Aurora kinases.
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    • 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
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    • Hannak, E.1    Kirkham, M.2    Hyman, A.A.3    Oegema, K.4
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    • Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis
    • In the Drosophila nervous system, Aurora A is shown to be required for the asymmetric localization of the cell-fate determinant Numb. Furthermore, cells expressing a mutant Aurora A protein displayed defects in spindle morphology, presumably because their centrosomes failed to recruit γ-tubulin and other centrosomal proteins. Thus, Aurora A is implicated in both centrosome maturation and cell-fate determination.
    • 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 In the Drosophila nervous system, Aurora A is shown to be required for the asymmetric localization of the cell-fate determinant Numb. Furthermore, cells expressing a mutant Aurora A protein displayed defects in spindle morphology, presumably because their centrosomes failed to recruit γ-tubulin and other centrosomal proteins. Thus, Aurora A is implicated in both centrosome maturation and cell-fate determination.
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    • Berdnik, D.1    Knoblich, J.A.2
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    • Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
    • By RNAi, Aurora A is shown to be required for multiple aspects of centrosome structure in Drosophila embryos and cultured cell lines. Of particular interest, the protein D-TACC is identified as an interaction partner and substrate of Aurora A.
    • 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 By RNAi, Aurora A is shown to be required for multiple aspects of centrosome structure in Drosophila embryos and cultured cell lines. Of particular interest, the protein D-TACC is identified as an interaction partner and substrate of Aurora A.
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    • Giet, R.1    Mclean, D.2    Descamps, S.3    Lee, M.J.4    Raff, J.W.5    Prigent, C.6    Glover, D.M.7
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    • Phospho-regulation of kinetochore-microtubule attachments by the aurora kinase ipl1p
    • A very thorough study identifying the protein Dam1p and several other kinetochore components as likely physiological substrates of Ipl1p in S. cerevisiae. Although no obvious orthologue of Dam1 has yet been found in mammals, Aurora B will certainly emerge as a key regulator of kinetochore-MT interactions in all eukaryotes.
    • Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J., Yates J.R., Chan C.S., Drubin D.G., Barnes G. Phospho-regulation of kinetochore-microtubule attachments by the aurora kinase ipl1p. Cell. 111:2002;163-172 A very thorough study identifying the protein Dam1p and several other kinetochore components as likely physiological substrates of Ipl1p in S. cerevisiae. Although no obvious orthologue of Dam1 has yet been found in mammals, Aurora B will certainly emerge as a key regulator of kinetochore-MT interactions in all eukaryotes.
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    • Cheeseman, I.M.1    Anderson, S.2    Jwa, M.3    Green, E.M.4    Kang, J.5    Yates, J.R.6    Chan, C.S.7    Drubin, D.G.8    Barnes, G.9
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    • Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
    • This key paper proposes a provocative model for the role of the budding yeast Aurora kinase Ipl1p. It shows that Ipl1p promotes MT turnover (and checkpoint activation) at mono-oriented chromosomes until a stable bi-oriented attachment generates tension.
    • Tanaka T.U., Rachidi N., Janke C., Pereira G., Galova M., Schiebel E., Stark M.J., 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 This key paper proposes a provocative model for the role of the budding yeast Aurora kinase Ipl1p. It shows that Ipl1p promotes MT turnover (and checkpoint activation) at mono-oriented chromosomes until a stable bi-oriented attachment generates tension.
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    • 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
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    • The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis
    • Expression of a dominant-negative Aurora B mutant in mammalian cells is shown to cause the depletion of motor proteins (dynein and CENP-E) from kinetochores, resulting in defects in both chromosome movement and spindle checkpoint.
    • Murata-Hori M., Wang Y. The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis. Curr Biol. 12:2002;894-899 Expression of a dominant-negative Aurora B mutant in mammalian cells is shown to cause the depletion of motor proteins (dynein and CENP-E) from kinetochores, resulting in defects in both chromosome movement and spindle checkpoint.
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    • Murata-Hori, M.1    Wang, Y.2
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    • 0037018844 scopus 로고    scopus 로고
    • Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
    • Using antibodies to interfere with Aurora B function in Xenopus egg extracts the authors demonstrate that Aurora B is required for both the establishment and the maintenance of the spindle checkpoint. Their data also suggest that Aurora B activity regulates MT 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 Using antibodies to interfere with Aurora B function in Xenopus egg extracts the authors demonstrate that Aurora B is required for both the establishment and the maintenance of the spindle checkpoint. Their data also suggest that Aurora B activity regulates MT dynamics.
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    • Kallio, M.J.1    Mccleland, M.L.2    Stukenberg, P.T.3    Gorbsky, G.J.4
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    • S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response
    • •]).
    • •]).
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    • Petersen, J.1    Hagan, I.M.2
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    • The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly
    • A careful study on the localization, by time-lapse microscopy, of the yeast Ipl1p Aurora kinase. It leads the authors to propose that Ipl1p regulates both the kinetochore and interpolar MT plus ends.
    • 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 A careful study on the localization, by time-lapse microscopy, of the yeast Ipl1p Aurora kinase. It leads the authors to propose that Ipl1p regulates both the kinetochore and interpolar MT plus ends.
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    • Buvelot, S.1    Tatsutani, S.Y.2    Vermaak, D.3    Biggins, S.4
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    • Both midzone and astral microtubules are involved in the delivery of cytokinesis signals: Insights from the mobility of aurora B
    • This study on the dynamics of Aurora B, using photobleaching experiments, indicates that Aurora B may reach the MT midzone by both centromere-dependent and independent pathways. It is inferred that the signaling pathways for cytokinesis may utilize both central spindle MTs and astral MTs.
    • Murata-Hori M., Wang Y.L. 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;45-53 This study on the dynamics of Aurora B, using photobleaching experiments, indicates that Aurora B may reach the MT midzone by both centromere-dependent and independent pathways. It is inferred that the signaling pathways for cytokinesis may utilize both central spindle MTs and astral MTs.
    • (2002) J Cell Biol , vol.159 , pp. 45-53
    • Murata-Hori, M.1    Wang, Y.L.2
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.