Journal Article


The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing

Abstract

Improperly attached kinetochores activate the spindle assembly checkpoint (SAC) and by an unknown mechanism catalyze 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 signaling and SAC silencing.

Attached files

Authors

Lischetti, Tiziana
Zhang Gang
Sedgwick, Garry G.
Bolanos-Garcia, Victor M.
Nilsson, Jakob

Oxford Brookes departments

Department of Biological and Medical Sciences

Dates

Year of publication: 2014
Date of RADAR deposit: 2019-07-31


Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License


Related resources

This RADAR resource is the Accepted Manuscript of The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing

Details

  • Owner: Joseph Ripp
  • Collection: Outputs
  • Version: 1 (show all)
  • Status: Live