Aurora‐C kinase is a novel chromosomal passenger protein that can complement Aurora‐B kinase function in mitotic cells

Sasai, Kaori; Katayama, Hiroshi; Stenoien, David L.; Fujii, Satoshi; Honda, Reiko; Kimura, Masashi; Okano, Yukio; Tatsuka, Masaaki; Suzuki, Fumio; Nigg, Erich A.; Earnshaw, William C.; Brinkley, William R.; Sen, Subrata

doi:10.1002/cm.20039

Cited by 251 publications

(239 citation statements)

References 29 publications

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“…Recently, it has been demonstrated that Aurora-C is a new member of the chromosomal passenger proteins interacting, similarly to Aurora-B, with INCENP and survivin, thus contributing to the regulation of chromosome segregation and cytokinesis 22,41 . In this context, it is worthwhile to mention that Aurora-B and C share the highest degree of sequence overlap with about 83% sequence identity whereas the kinases C and A share about 71% sequence identity.…”

Section: Discussionmentioning

confidence: 99%

Expression of Aurora kinases in human thyroid carcinoma cell lines and tissues

Ulisse

Delcros²,

Baldini

et al. 2006

Intl Journal of Cancer

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The Aurora kinases are involved in the regulation of cell cycle progression, and alterations in their expression have been shown to associate with cell malignant transformation. In the present study, we demonstrated that human thyrocytes express all 3 Aurora kinases (A, B and C) at both protein and mRNA level and this expression is cell cycle-regulated. An increase in the protein level of the 3 kinases was found, with respect to normal human thyrocytes (HTU5), in the human cell lines derived from follicular (FTC-133), papillary (B-CPAP) and anaplastic (8305C) thyroid carcinomas, but not in cells derived from a follicular adenoma (HTU42). These observations were mirrored in RT-PCR experiments for Aurora-A and B. In contrast, Aurora-C mRNA levels were not significantly different among the different cell types analyzed, suggesting that posttranscriptional mechanism(s) modulate its expression. The expression at the protein level of all 3 Aurora kinases was significantly higher in 3 thyroid papillary carcinomas with respect to normal matched tissues obtained from the same patients. Similar modifications, at the mRNA level, could be observed in 7 papillary carcinoma tissues for Aurora-A and B, but not for Aurora-C. In conclusion, we demonstrated that normal human thyrocytes express all 3 members of the Aurora kinase family, and their expression is amplified in malignant thyroid cell lines and tissues. These results suggest that the Aurora kinases may play a relevant role in malignant thyroid cancers, and may represent a putative therapeutic target for thyroid neoplasms

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Section: Discussionmentioning

confidence: 99%

Expression of Aurora kinases in human thyroid carcinoma cell lines and tissues

Ulisse

Delcros²,

Baldini

et al. 2006

Intl Journal of Cancer

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“…Aurora C was shown to localize like a chromosomal passenger protein, but it is expressed at lower levels than Aurora B and might be func- tionally redundant with Aurora B (Li et al, 2004;Sasai et al, 2004). However, simultaneous knockdown of INCENP and Aurora C or INCENP, Aurora C, and Aurora B followed by rescue with GFP-INCENP 1-58 resulted in centromere localization of the ternary INCENP 1-58 -Survivin-Borealin complex, excluding a compensatory role for Aurora C (Supplemental Figure S2, middle and bottom rows).…”

Section: Ectopic Gfp-incenp 1-58 Can Target Survivin and Borealin Butmentioning

confidence: 99%

Centromere Targeting of the Chromosomal Passenger Complex Requires a Ternary Subcomplex of Borealin, Survivin, and the N-Terminal Domain of INCENP

Klein

Nigg

Grüneberg

2006

MBoC

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162

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The chromosomal passenger complex (CPC), consisting of the serine/threonine kinase Aurora B, the inner centromere protein INCENP, Survivin, and Borealin/DasraB, has essential functions at the centromere in ensuring correct chromosome alignment and segregation. Despite observations that small interfering RNA-mediated knockdown of any one member of the CPC abolishes localization of the other subunits, it remains unclear how the complex is targeted to the centromere. We have now identified a ternary subcomplex of the CPC comprising Survivin, Borealin, and the N-terminal 58 amino acids of INCENP in vitro and in vivo. This subcomplex was found to be essential and sufficient for targeting to the centromere. Notably, Aurora B kinase, the enzymatic core of the CPC, was not required for centromere localization of the subcomplex. We demonstrate that CPC targeting to the centromere does not depend on CENP-A and hMis12, two core components for kinetochore/centromere assembly, and provide evidence that the CPC may be directed to centromeric DNA directly via the Borealin subunit. Our findings thus establish a functional module within the CPC that assembles on the N terminus of INCENP and controls centromere recruitment.

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“…1D) and the overexpression of Aurora-C-WT has no significant effects. 6,7,9,16 In contrast, ectopic expression of Aurora-C-T191D specifically induces morphological changes in U2OS cells (Fig. 1D).…”

mentioning

confidence: 94%

“…4,5 Overexpression studies with Aurora-C suggest that it has overlapping functions with Aurora-B in mitosis and with Aurora-A in interphase. [6][7][8][9] Because the three mammalian Aurora paralogues are very similar in sequence, it is possible that these results are artificial and do not represent the true physiological functions of Aurora-C. So far, the studies were mainly based on the ectopic expression of kinase-inactive Aurora-C mutants and Aurora-C-WT.…”

mentioning

confidence: 99%