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The roles for the BUB3-BUB1 complex in S phase.
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Small sequence differences in Bub1 and BubR1 direct Bub3 to different phosphorylated targets in the spindle assembly checkpoint signaling cascade.
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The integrity of the mitotic checkpoint complex depends on the specific recognition between BubR1 and Bub3, for which the BubR1 Gle2 binding sequence motif is essential.
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We show that kinetochore recruitment of BUBR1 and BUB3 by BUB1 is dispensable for SAC activation
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a mutual antagonism exists between Bub3 and dynein to ensure optimal KT-MT attachments
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the mechanisms of BUB3 in mitotic checkpoint signaling
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Data show sequential multisite regulation of the microtubule-associated protein KNL1-kinase-adaptor complex BUB1/BUB3 interaction.
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Data indicate that cell cycle protein Bub3-mediated kinetochore recruitment of BubR1 kinase enhances mitotic checkpoint signaling.
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Results suggest that these USP7-dependent effects are mediated by decreased levels of spindle assembly checkpoint (SAC) component Bub3.
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Mutations targeting the Bub3 interface prevent kinetochore recruitment of the SAC kinase Bub1. Crucially, they also cause a checkpoint defect, showing that recognition of phosphorylated targets by Bub3 is required for checkpoint signaling
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Results showed that neither variants in BUB3 nor variants in MAD2L1 caused any significant effect on the risk of breast cancer
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Mutations in BUB1 and BUB3 cause mosaic variegated aneuploidy and increase the risk of colorectal cancer at a young age.
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These results indicate that Bub3 and Cdc20 play additional roles in the integration of cell cycle arrest as transcriptional repressors.
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Allelic loss at 10q26 in osteosarcoma is reported in the region of BUB3.
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subpopulation of dynein, containing the DYNLT3 light chain, may be important for chromosome congression, in addition to having a role in the transport of checkpoint proteins from the kinetochore to the spindle pole
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Using RNA interference and high-resolution microscopy, we analyzed kinetochore-microtubule attachments in Bub3-depleted cells and compared them to those in Bub1- or BubR1-depleted cells.
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Results suggest a novel molecular mechanism leading to aneuploidy involving interference of TAp73alpha with Bub1 and Bub3 resulting in an altered mitotic checkpoint.
