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- W2104480930 abstract "Accurate chromosome segregation during mitosis is temporally and spatially coordinated by fidelity-monitoring checkpoint systems. Deficiencies in these checkpoint systems can lead to chromosome segregation errors and aneuploidy and promote tumorigenesis. We report that the TRAF-interacting protein (TRAIP), a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation, was localized close to mitotic chromosomes. Its functional inactivation in HeLa cells by siRNAs decreased the time of early mitosis progression from nuclear envelope breakdown to anaphase onset and increased the percentages of chromosome alignment defects in metaphase and lagging chromosomes in anaphase compared to control cells. The decrease in progression time was corrected by the expression of wild-type but not by an ubiquitin ligase deficient form of TRAIP. TRAIP-depleted cells by-passed taxol-induced mitotic arrest, and significantly reduced kinetochore levels of MAD2 but not of other spindle checkpoint proteins in the presence of nocodazole. These results imply that TRAIP regulates the spindle assembly checkpoint, MAD2 abundance at kinetochores and the accurate cellular distribution of chromosomes. The TRAIP ubiquitin ligase activity is functionally required for the spindle assembly checkpoint control." @default.
- W2104480930 created "2016-06-24" @default.
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- W2104480930 date "2014-01-01" @default.
- W2104480930 modified "2023-10-10" @default.
- W2104480930 title "The TRAF-interacting protein (TRAIP) is a regulator of the spindle assembly checkpoint" @default.
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- W2104480930 doi "https://doi.org/10.1242/jcs.152579" @default.
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