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1
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0035235736
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Mitotic kinases as regulators of cell division and its checkpoints
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Nigg E.A. Mitotic kinases as regulators of cell division and its checkpoints. Nat Rev Mol Cell Biol. 2:2001;21-32.
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(2001)
Nat Rev Mol Cell Biol
, vol.2
, pp. 21-32
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Nigg, E.A.1
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2
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0038341158
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The Aurora kinases: Role in cell transformation and tumorigenesis
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A comprehensive review focusing on the growing evidence linking Aurora kinase deregulation to carcinogenesis.
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Katayama H., Brinkley W.R., Sen S. The Aurora kinases: role in cell transformation and tumorigenesis. Cancer Metastasis Rev. 22:2003;451-464 A comprehensive review focusing on the growing evidence linking Aurora kinase deregulation to carcinogenesis.
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(2003)
Cancer Metastasis Rev
, vol.22
, pp. 451-464
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Katayama, H.1
Brinkley, W.R.2
Sen, S.3
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3
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0035252654
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Chromosomal passengers and the (aurora) ABCs of mitosis
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Adams R.R., Carmena M., Earnshaw W.C. Chromosomal passengers and the (aurora) ABCs of mitosis. Trends Cell Biol. 11:2001;49-54.
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(2001)
Trends Cell Biol
, vol.11
, pp. 49-54
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Adams, R.R.1
Carmena, M.2
Earnshaw, W.C.3
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4
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0037044846
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Crystal structure of aurora-2, an oncogenic serine/threonine kinase
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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.
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(2002)
J Biol Chem
, vol.277
, pp. 42419-42422
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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
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5
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0037048279
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On the role of aurora-A in centrosome function
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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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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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(2002)
Oncogene
, vol.21
, pp. 6175-6183
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Dutertre, S.1
Descamps, S.2
Prigent, C.3
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6
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0037046861
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Chromosome dynamics: New light on aurora B kinase function
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An excellent, concise review on the multiple functions of Aurora B.
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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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(2002)
Curr Biol
, vol.12
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Shannon, K.B.1
Salmon, E.D.2
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7
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0037180488
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Identification of phosphorylated residues that affect the activity of the mitotic kinase Aurora-A
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••]). 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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••]). 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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(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 15440-15445
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Littlepage, L.E.1
Wu, H.2
Andresson, T.3
Deanehan, J.K.4
Amundadottir, L.T.5
Ruderman, J.V.6
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8
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0842299091
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Identification of novel phosphorylation sites on Xenopus laevis Aurora A and analysis of phosphopeptide enrichment by immobilized metal-affinity chromatography
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••]). 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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••]). 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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(2003)
Mol Cell Proteomics
, vol.2
, pp. 1055-1067
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Haydon, C.E.1
Eyers, P.A.2
Aveline-Wolf, L.D.3
Resing, K.A.4
Maller, J.L.5
Ahn, N.G.6
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10
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0037341906
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A Ran signalling pathway mediated by the mitotic kinase Aurora A in spindle assembly
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••]).
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••]).
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(2003)
Nat Cell Biol
, vol.5
, pp. 242-248
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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
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11
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0037446847
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A novel mechanism for activation of the protein kinase aurora a
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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., 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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(2003)
Curr Biol
, vol.13
, pp. 691-697
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Eyers, P.A.1
Erikson, E.2
Chen, L.G.3
Maller, J.L.4
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12
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0242330123
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Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
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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., 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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(2003)
Mol Cell
, vol.12
, pp. 851-862
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Bayliss, R.1
Sardon, T.2
Vernos, I.3
Conti, E.4
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14
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0036714512
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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
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•]). In addition, overexpression of Aurora A was shown to transform NIH 3T3 cells.
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•]). In addition, overexpression of Aurora A was shown to transform NIH 3T3 cells.
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(2002)
Genes Dev
, vol.16
, pp. 2274-2285
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Littlepage, L.E.1
Ruderman, J.V.2
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15
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0037160088
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Aurora-A kinase interacting protein (AIP), a novel negative regulator of human Aurora-A kinase
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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., 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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(2002)
J Biol Chem
, vol.277
, pp. 45558-45565
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Kiat, L.S.1
Hui, K.M.2
Gopalan, G.3
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17
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0038070181
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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
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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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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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(2003)
J Cell Biol
, vol.161
, pp. 229-236
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Romano, A.1
Guse, A.2
Krascenicova, I.3
Schnabel, H.4
Schnabel, R.5
Glotzer, M.6
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18
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0035810919
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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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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.
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(2001)
Curr Biol
, vol.11
, pp. 886-890
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Wheatley, S.P.1
Carvalho, A.2
Vagnarelli, P.3
Earnshaw, W.C.4
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21
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0035956434
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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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Kang J., 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.
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(2001)
J Cell Biol
, vol.155
, pp. 763-774
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Kang, J.1
Cheeseman, I.M.2
Kallstrom, G.3
Velmurugan, S.4
Barnes, G.5
Chan, C.S.6
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22
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0037008684
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Phosphorylation of the carboxyl terminus of inner centromere protein (INCENP) by the Aurora B Kinase stimulates Aurora B kinase activity
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•]).
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•]).
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(2002)
J Biol Chem
, vol.277
, pp. 27577-27580
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Bishop, J.D.1
Schumacher, J.M.2
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23
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0036732808
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Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
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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.
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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.
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(2002)
Mol Biol Cell
, vol.13
, pp. 3064-3077
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Bolton, M.A.1
Lan, W.2
Powers, S.E.3
Mccleland, M.L.4
Kuang, J.5
Stukenberg, P.T.6
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24
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0037414775
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Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells
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Chen J., Jin S., Tahir S.K., Zhang H., Liu X., Sarthy A.V., McGonigal T.P., Liu Z., Rosenberg S.H., Ng S.C. Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells. J Biol Chem. 278:2002;486-490.
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(2002)
J Biol Chem
, vol.278
, pp. 486-490
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Chen, J.1
Jin, S.2
Tahir, S.K.3
Zhang, H.4
Liu, X.5
Sarthy, A.V.6
Mcgonigal, T.P.7
Liu, Z.8
Rosenberg, S.H.9
Ng, S.C.10
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25
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0034604354
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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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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.
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(2000)
Cell
, vol.102
, pp. 279-291
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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
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26
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0035911159
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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
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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. 152:2001;669-682.
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(2001)
J Cell Biol
, vol.152
, pp. 669-682
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Giet, R.1
Glover, D.M.2
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27
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0036142218
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Mitotic phosphorylation of histone H3: Spatio-temporal regulation by mammalian Aurora kinases
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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., 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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(2002)
Mol Cell Biol
, vol.22
, pp. 874-885
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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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28
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0035945340
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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., 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.
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(2001)
J Cell Biol
, vol.155
, pp. 1147-1157
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Zeitlin, S.G.1
Shelby, R.D.2
Sullivan, K.F.3
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29
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0037105758
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Increased mitotic phosphorylation of histone H3 attributable to AIM-1/Aurora-B overexpression contributes to chromosome number instability
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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., 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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(2002)
Cancer Res
, vol.62
, pp. 5168-5177
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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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31
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0035945342
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Aurora-A kinase is required for centrosome maturation in Caenorhabditis elegans
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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.
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(2001)
J Cell Biol
, vol.155
, pp. 1109-1116
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Hannak, E.1
Kirkham, M.2
Hyman, A.A.3
Oegema, K.4
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32
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0037117408
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Drosophila Aurora-A is required for centrosome maturation and actin-dependent asymmetric protein localization during mitosis
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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., 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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(2002)
Curr Biol
, vol.12
, pp. 640-647
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Berdnik, D.1
Knoblich, J.A.2
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33
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0037017398
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Drosophila Aurora A kinase is required to localize D-TACC to centrosomes and to regulate astral microtubules
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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., 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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(2002)
J Cell Biol
, vol.156
, pp. 437-451
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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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34
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0036569124
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Centrosomes and cancer: Lessons from a TACC
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A concise review on the intriguing TACC family of proteins, with a special emphasis on their possible role in malignant transformation.
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Raff J.W. Centrosomes and cancer: lessons from a TACC. Trends Cell Biol. 12:2002;222-225 A concise review on the intriguing TACC family of proteins, with a special emphasis on their possible role in malignant transformation.
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(2002)
Trends Cell Biol
, vol.12
, pp. 222-225
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Raff, J.W.1
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35
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0037459109
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Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling
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A comprehensive and authoritative review of our understanding of kinetochore assembly and checkpoint signaling.
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Cleveland D.W., Mao Y., Sullivan K.F. Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling. Cell. 112:2003;407-421 A comprehensive and authoritative review of our understanding of kinetochore assembly and checkpoint signaling.
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(2003)
Cell
, vol.112
, pp. 407-421
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Cleveland, D.W.1
Mao, Y.2
Sullivan, K.F.3
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36
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0035577762
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The budding yeast protein kinase Ipl1/Aurora allows the absence of tension to activate the spindle checkpoint
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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. 15:2001;3118-3129.
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(2001)
Genes Dev
, vol.15
, pp. 3118-3129
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Biggins, S.1
Murray, A.W.2
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37
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0037131572
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Phospho-regulation of kinetochore-microtubule attachments by the aurora kinase ipl1p
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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., 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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(2002)
Cell
, vol.111
, pp. 163-172
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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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38
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0036178929
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Evidence that the Ipl1-Sli15 (Aurora kinase-INCENP) complex promotes chromosome bi-orientation by altering kinetochore-spindle pole connections
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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., 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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(2002)
Cell
, vol.108
, pp. 317-329
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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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39
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0037018843
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The kinase activity of Aurora B is required for kinetochore-microtubule interactions during mitosis
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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., 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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(2002)
Curr Biol
, vol.12
, pp. 894-899
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Murata-Hori, M.1
Wang, Y.2
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41
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0037018844
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Inhibition of aurora B kinase blocks chromosome segregation, overrides the spindle checkpoint, and perturbs microtubule dynamics in mitosis
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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., 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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(2002)
Curr Biol
, vol.12
, pp. 900-905
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Kallio, M.J.1
Mccleland, M.L.2
Stukenberg, P.T.3
Gorbsky, G.J.4
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42
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0038376119
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Survivin is required for a sustained spindle checkpoint arrest in response to lack of tension
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Lens, S.M.1
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S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response
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Hauf, S.1
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47
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The budding yeast Ipl1/Aurora protein kinase regulates mitotic spindle disassembly
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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., 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
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Both midzone and astral microtubules are involved in the delivery of cytokinesis signals: Insights from the mobility of aurora B
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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.
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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.
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J Cell Biol
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Murata-Hori, M.1
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Central spindle assembly and cytokinesis require a kinesin-like protein/RhoGAP complex with microtubule bundling activity
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A complex - consisting of a kinesin-related motor protein and a GAP for small GTPases - is here shown to be conserved between C. elegans and human cells. This complex was required for central spindle formation in vivo and able to promote the bundling of MTs in vitro. Hence, the term 'centralspindlin' was coined to describe this evolutionarily conserved regulator of cytokinesis.
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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 A complex - consisting of a kinesin-related motor protein and a GAP for small GTPases - is here shown to be conserved between C. elegans and human cells. This complex was required for central spindle formation in vivo and able to promote the bundling of MTs in vitro. Hence, the term 'centralspindlin' was coined to describe this evolutionarily conserved regulator of cytokinesis.
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Mishima, M.1
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Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP during cytokinesis
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Dev Cell
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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 Jr. et al., W.S.10
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Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process
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J Biol Chem
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Goto, H.1
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Inagaki, M.8
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54
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0042093747
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Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human
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Human Aurora A (STK15) displays a polymorphism at codon 31 (Ile/Phe) and the data demonstrate selective amplification of the Ile allele in colorectal cancers. Moreover, the Ile variant shows reduced interaction with a ubiquitin-conjugating enzyme, which may help explain its selection.
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Ewart-Toland A., Briassouli P., De Koning J.P., Mao J.H., Yuan J., Chan F., MacCarthy-Morrogh L., Ponder B.A., Nagase H., Burn J.et al. Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human. Nat Genet. 34:2003;403-412 Human Aurora A (STK15) displays a polymorphism at codon 31 (Ile/Phe) and the data demonstrate selective amplification of the Ile allele in colorectal cancers. Moreover, the Ile variant shows reduced interaction with a ubiquitin-conjugating enzyme, which may help explain its selection.
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Nat Genet
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Ewart-Toland, A.1
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De Koning, J.P.3
Mao, J.H.4
Yuan, J.5
Chan, F.6
Maccarthy-Morrogh, L.7
Ponder, B.A.8
Nagase, H.9
Burn, J.10
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57
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Centrosome aberrations: Cause or consequence of cancer progression?
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This review summarizes the mechanisms that can give rise to structural and numerical centrosome abnormalities in human tumors. Furthermore, it discusses the intimate relationship that exists between centrosome abnormalitites, cell-division errors, and chromosomal instability.
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Nigg E.A. Centrosome aberrations: cause or consequence of cancer progression? Nat Rev Cancer. 2:2002;815-825 This review summarizes the mechanisms that can give rise to structural and numerical centrosome abnormalities in human tumors. Furthermore, it discusses the intimate relationship that exists between centrosome abnormalitites, cell-division errors, and chromosomal instability.
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Nigg, E.A.1
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G1 tetraploidy checkpoint and the suppression of tumorigenesis
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1 tetraploidy checkpoint arrests and/or eliminates those cells that arise through faulty division processes. Although the molecular mechanisms underlying the latter checkpoint remain poorly understood, both the p53 and pRb tumor suppressor proteins appear to be involved.
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1 tetraploidy checkpoint arrests and/or eliminates those cells that arise through faulty division processes. Although the molecular mechanisms underlying the latter checkpoint remain poorly understood, both the p53 and pRb tumor suppressor proteins appear to be involved.
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J Cell Biochem
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Margolis, R.L.1
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AIM-1: A mammalian midbody-associated protein required for cytokinesis
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Mendez R., Richter J.D. Translational control by CPEB: a means to the end. Nat Rev Mol Cell Biol. 2:2001;521-529.
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0041885288
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Interaction of Aurora-A and centrosomin at the microtubule-nucleating site in Drosophila and mammalian cells
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In Drosophila, the protein centrosomin (CNN) and Aurora-A were found to be mutually dependent on each other for centrosome localization. Moreover, centrosomin was shown to interact with γ-tubulin ring complexes through its N terminus and to Aurora-A through its C terminus. To extend these findings to other organisms, it would be important to identify functional homologues of Drosophila centrosomin in other species.
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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;757-763 In Drosophila, the protein centrosomin (CNN) and Aurora-A were found to be mutually dependent on each other for centrosome localization. Moreover, centrosomin was shown to interact with γ-tubulin ring complexes through its N terminus and to Aurora-A through its C terminus. To extend these findings to other organisms, it would be important to identify functional homologues of Drosophila centrosomin in other species.
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J Cell Biol
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Terada, Y.1
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0141429171
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Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells
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The LIM protein Ajuba is described as a binding partner of Aurora A at the centrosomes in human cells. Binding of Ajuba is reported to stimulate autophosphorylation and activation of Aurora A both in vivo and in vitro. Furthermore, the data suggest that the Aurora-A-Ajuba complex is required for both centrosome maturation and entry into mitosis.
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Hirota T., Kunitoku N., Sasayama T., Marumoto T., Zhang D., Nitta M., Hatakeyama K., Saya H. Aurora-A and an interacting activator, the LIM protein Ajuba, are required for mitotic commitment in human cells. Cell. 114:2003;585-598 The LIM protein Ajuba is described as a binding partner of Aurora A at the centrosomes in human cells. Binding of Ajuba is reported to stimulate autophosphorylation and activation of Aurora A both in vivo and in vitro. Furthermore, the data suggest that the Aurora-A-Ajuba complex is required for both centrosome maturation and entry into mitosis.
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(2003)
Cell
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Hirota, T.1
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Sasayama, T.3
Marumoto, T.4
Zhang, D.5
Nitta, M.6
Hatakeyama, K.7
Saya, H.8
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