Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B

B. W. Lin; Y. C. Wang; P. Y. Chang-Liao; Y. J. Lin; S. T. Yang; J. H. Tsou; K. C. Chang; Y. W. Liu; J. T. Tseng; C. T. Lee; J. C. Lee; L. Y. Hung

doi:10.1038/cddis.2014.37

Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B

B. W. Lin, Y. C. Wang, P. Y. Chang-Liao, Y. J. Lin, S. T. Yang, J. H. Tsou, K. C. Chang, Y. W. Liu, J. T. Tseng, C. T. Lee, J. C. Lee, L. Y. Hung

研究成果: Article › 同行評審

9 引文斯高帕斯（Scopus）

摘要

The chromosomal passenger complex (CPC) plays a pivotal role in controlling accurate chromosome segregation and cytokinesis during cell division. Aurora-B, one of the chromosomal passenger proteins, is important for the mitotic spindle assembly checkpoint (SAC). Previous reports noted that Aurora-C is predominantly expressed in male germ cells and has the same subcellular localization as Aurora-B. Increasing evidence indicates that Aurora-C is overexpressed in many somatic cancers, although its function is uncertain. Our previous study showed that the aberrant expression of Aurora-C increases the tumorigenicity of cancer cells. Here, we demonstrate that overexpressed Aurora-C displaces the centromeric localization of CPCs, including INCENP, survivin, and Aurora-B. When cells were treated with nocodazole to turn on SAC, both the Aurora-B protein stability and kinase activity were affected by overexpressed Aurora-C. As a result, the activation of spindle checkpoint protein, BubR1, and phosphorylation of histone H3 and MCAK were also eliminated in Aurora-C-overexpressing cells. Thus, our results suggest that aberrantly expressed Aurora-C in somatic cancer cells may impair SAC by displacing the centromeric localization of CPCs.

原文	English
文章編號	e1106
期刊	Cell Death and Disease
卷	5
發行號	3
DOIs	https://doi.org/10.1038/cddis.2014.37
出版狀態	Published - 2014 3月

All Science Journal Classification (ASJC) codes

免疫學
細胞與分子神經科學
細胞生物學
癌症研究

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10.1038/cddis.2014.37

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title = "Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B",

abstract = "The chromosomal passenger complex (CPC) plays a pivotal role in controlling accurate chromosome segregation and cytokinesis during cell division. Aurora-B, one of the chromosomal passenger proteins, is important for the mitotic spindle assembly checkpoint (SAC). Previous reports noted that Aurora-C is predominantly expressed in male germ cells and has the same subcellular localization as Aurora-B. Increasing evidence indicates that Aurora-C is overexpressed in many somatic cancers, although its function is uncertain. Our previous study showed that the aberrant expression of Aurora-C increases the tumorigenicity of cancer cells. Here, we demonstrate that overexpressed Aurora-C displaces the centromeric localization of CPCs, including INCENP, survivin, and Aurora-B. When cells were treated with nocodazole to turn on SAC, both the Aurora-B protein stability and kinase activity were affected by overexpressed Aurora-C. As a result, the activation of spindle checkpoint protein, BubR1, and phosphorylation of histone H3 and MCAK were also eliminated in Aurora-C-overexpressing cells. Thus, our results suggest that aberrantly expressed Aurora-C in somatic cancer cells may impair SAC by displacing the centromeric localization of CPCs.",

author = "Lin, {B. W.} and Wang, {Y. C.} and Chang-Liao, {P. Y.} and Lin, {Y. J.} and Yang, {S. T.} and Tsou, {J. H.} and Chang, {K. C.} and Liu, {Y. W.} and Tseng, {J. T.} and Lee, {C. T.} and Lee, {J. C.} and Hung, {L. Y.}",

note = "Funding Information: Acknowledgements. We thank Mr. Buford Pruitt Jr. and Enago (www.ena-go.tw) for the English language review. This work was supported by grants NSC101-2325-B-006-001 and NSC102-2325-B-006-001 from the National Science Council; Project of Promoting Academic Excellence and Developing World Class Research Centers (C006); Infectious Disease and Signaling Research Center, National Cheng Kung University; and National Cheng Kung University Hospital (NCKUH-10102063, NCKUH-10202004).",

year = "2014",

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T1 - Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B

AU - Lin, B. W.

AU - Wang, Y. C.

AU - Chang-Liao, P. Y.

AU - Lin, Y. J.

AU - Yang, S. T.

AU - Tsou, J. H.

AU - Chang, K. C.

AU - Liu, Y. W.

AU - Tseng, J. T.

AU - Lee, C. T.

AU - Lee, J. C.

AU - Hung, L. Y.

N1 - Funding Information: Acknowledgements. We thank Mr. Buford Pruitt Jr. and Enago (www.ena-go.tw) for the English language review. This work was supported by grants NSC101-2325-B-006-001 and NSC102-2325-B-006-001 from the National Science Council; Project of Promoting Academic Excellence and Developing World Class Research Centers (C006); Infectious Disease and Signaling Research Center, National Cheng Kung University; and National Cheng Kung University Hospital (NCKUH-10102063, NCKUH-10202004).

PY - 2014/3

Y1 - 2014/3

N2 - The chromosomal passenger complex (CPC) plays a pivotal role in controlling accurate chromosome segregation and cytokinesis during cell division. Aurora-B, one of the chromosomal passenger proteins, is important for the mitotic spindle assembly checkpoint (SAC). Previous reports noted that Aurora-C is predominantly expressed in male germ cells and has the same subcellular localization as Aurora-B. Increasing evidence indicates that Aurora-C is overexpressed in many somatic cancers, although its function is uncertain. Our previous study showed that the aberrant expression of Aurora-C increases the tumorigenicity of cancer cells. Here, we demonstrate that overexpressed Aurora-C displaces the centromeric localization of CPCs, including INCENP, survivin, and Aurora-B. When cells were treated with nocodazole to turn on SAC, both the Aurora-B protein stability and kinase activity were affected by overexpressed Aurora-C. As a result, the activation of spindle checkpoint protein, BubR1, and phosphorylation of histone H3 and MCAK were also eliminated in Aurora-C-overexpressing cells. Thus, our results suggest that aberrantly expressed Aurora-C in somatic cancer cells may impair SAC by displacing the centromeric localization of CPCs.

AB - The chromosomal passenger complex (CPC) plays a pivotal role in controlling accurate chromosome segregation and cytokinesis during cell division. Aurora-B, one of the chromosomal passenger proteins, is important for the mitotic spindle assembly checkpoint (SAC). Previous reports noted that Aurora-C is predominantly expressed in male germ cells and has the same subcellular localization as Aurora-B. Increasing evidence indicates that Aurora-C is overexpressed in many somatic cancers, although its function is uncertain. Our previous study showed that the aberrant expression of Aurora-C increases the tumorigenicity of cancer cells. Here, we demonstrate that overexpressed Aurora-C displaces the centromeric localization of CPCs, including INCENP, survivin, and Aurora-B. When cells were treated with nocodazole to turn on SAC, both the Aurora-B protein stability and kinase activity were affected by overexpressed Aurora-C. As a result, the activation of spindle checkpoint protein, BubR1, and phosphorylation of histone H3 and MCAK were also eliminated in Aurora-C-overexpressing cells. Thus, our results suggest that aberrantly expressed Aurora-C in somatic cancer cells may impair SAC by displacing the centromeric localization of CPCs.

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Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B

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