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• W1974948367 abstract "Improperly attached kinetochores activate the spindle assembly checkpoint (SAC) and by an unknown mechanism catalyse the binding of two checkpoint proteins, Mad2 and BubR1, to Cdc20 forming the mitotic checkpoint complex (MCC). Here, to address the functional role of Cdc20 kinetochore localization in the SAC, we delineate the molecular details of its interaction with kinetochores. We find that BubR1 recruits the bulk of Cdc20 to kinetochores through its internal Cdc20 binding domain (IC20BD). We show that preventing Cdc20 kinetochore localization by removal of the IC20BD has a limited effect on the SAC because the IC20BD is also required for efficient SAC silencing. Indeed, the IC20BD can disrupt the MCC providing a mechanism for its role in SAC silencing. We thus uncover an unexpected dual function of the second Cdc20 binding site in BubR1 in promoting both efficient SAC signalling and SAC silencing. Kinetochores that fail to form bipolar attachments to the mitotic spindle delay chromosome segregation by BubR1 mediated inhibition of Cdc20. Lischetti et al.show that BubR1 recruits Cdc20 to the kinetochore via a domain that mediates both checkpoint activation and silencing." @default.
• W1974948367 created "2016-06-24" @default.
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• W1974948367 date "2014-12-08" @default.
• W1974948367 modified "2023-10-18" @default.
• W1974948367 title "The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing" @default.
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• W1974948367 doi "https://doi.org/10.1038/ncomms6563" @default.
• W1974948367 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25482201" @default.
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