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Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B
by
Tseng, J T
, Lee, J-C
, Wang, Y-C
, Chang-Liao, P-Y
, Lin, Y-J
, Lee, C-T
, Hung, L-Y
, Yang, S-T
, Chang, K-C
, Tsou, J-H
, Liu, Y-W
, Lin, B-W
in
631/80/641/2187
/ 631/80/82
/ 692/420/755
/ Antibodies
/ Aurora Kinase B - metabolism
/ Aurora Kinase C - genetics
/ Aurora Kinase C - metabolism
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Cell Movement
/ Cell Proliferation
/ Cell Survival
/ Centromere - enzymology
/ Chromosomal Proteins, Non-Histone - metabolism
/ Dose-Response Relationship, Drug
/ Female
/ HeLa Cells
/ Histones - metabolism
/ Humans
/ Immunology
/ Inhibitor of Apoptosis Proteins - metabolism
/ Kinesin - metabolism
/ Life Sciences
/ M Phase Cell Cycle Checkpoints - drug effects
/ Neoplasm Invasiveness
/ Nocodazole - pharmacology
/ Original
/ original-article
/ Phosphorylation
/ Protein-Serine-Threonine Kinases - metabolism
/ Proteolysis
/ Spindle Apparatus - drug effects
/ Spindle Apparatus - enzymology
/ Time Factors
/ Transfection
/ Up-Regulation
2014
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Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B
by
Tseng, J T
, Lee, J-C
, Wang, Y-C
, Chang-Liao, P-Y
, Lin, Y-J
, Lee, C-T
, Hung, L-Y
, Yang, S-T
, Chang, K-C
, Tsou, J-H
, Liu, Y-W
, Lin, B-W
in
631/80/641/2187
/ 631/80/82
/ 692/420/755
/ Antibodies
/ Aurora Kinase B - metabolism
/ Aurora Kinase C - genetics
/ Aurora Kinase C - metabolism
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Cell Movement
/ Cell Proliferation
/ Cell Survival
/ Centromere - enzymology
/ Chromosomal Proteins, Non-Histone - metabolism
/ Dose-Response Relationship, Drug
/ Female
/ HeLa Cells
/ Histones - metabolism
/ Humans
/ Immunology
/ Inhibitor of Apoptosis Proteins - metabolism
/ Kinesin - metabolism
/ Life Sciences
/ M Phase Cell Cycle Checkpoints - drug effects
/ Neoplasm Invasiveness
/ Nocodazole - pharmacology
/ Original
/ original-article
/ Phosphorylation
/ Protein-Serine-Threonine Kinases - metabolism
/ Proteolysis
/ Spindle Apparatus - drug effects
/ Spindle Apparatus - enzymology
/ Time Factors
/ Transfection
/ Up-Regulation
2014
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Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B
by
Tseng, J T
, Lee, J-C
, Wang, Y-C
, Chang-Liao, P-Y
, Lin, Y-J
, Lee, C-T
, Hung, L-Y
, Yang, S-T
, Chang, K-C
, Tsou, J-H
, Liu, Y-W
, Lin, B-W
in
631/80/641/2187
/ 631/80/82
/ 692/420/755
/ Antibodies
/ Aurora Kinase B - metabolism
/ Aurora Kinase C - genetics
/ Aurora Kinase C - metabolism
/ Biochemistry
/ Biomedical and Life Sciences
/ Cell Biology
/ Cell Culture
/ Cell Movement
/ Cell Proliferation
/ Cell Survival
/ Centromere - enzymology
/ Chromosomal Proteins, Non-Histone - metabolism
/ Dose-Response Relationship, Drug
/ Female
/ HeLa Cells
/ Histones - metabolism
/ Humans
/ Immunology
/ Inhibitor of Apoptosis Proteins - metabolism
/ Kinesin - metabolism
/ Life Sciences
/ M Phase Cell Cycle Checkpoints - drug effects
/ Neoplasm Invasiveness
/ Nocodazole - pharmacology
/ Original
/ original-article
/ Phosphorylation
/ Protein-Serine-Threonine Kinases - metabolism
/ Proteolysis
/ Spindle Apparatus - drug effects
/ Spindle Apparatus - enzymology
/ Time Factors
/ Transfection
/ Up-Regulation
2014
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Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B
Journal Article
Overexpression of Aurora-C interferes with the spindle checkpoint by promoting the degradation of Aurora-B
2014
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Overview
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.
Publisher
Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
Subject
/ Aurora Kinase B - metabolism
/ Aurora Kinase C - metabolism
/ Biomedical and Life Sciences
/ Chromosomal Proteins, Non-Histone - metabolism
/ Dose-Response Relationship, Drug
/ Female
/ Humans
/ Inhibitor of Apoptosis Proteins - metabolism
/ M Phase Cell Cycle Checkpoints - drug effects
/ Original
/ Protein-Serine-Threonine Kinases - metabolism
/ Spindle Apparatus - drug effects
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