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

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  • Tiziana Lischetti

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

  • Gang Zhang

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

  • Garry G. Sedgwick

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

  • Victor M. Bolanos-Garcia

    (Oxford Brookes University, Gipsy Lane, Headington)

  • Jakob Nilsson

    (The Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen)

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.

Suggested Citation

  • Tiziana Lischetti & Gang Zhang & Garry G. Sedgwick & Victor M. Bolanos-Garcia & Jakob Nilsson, 2014. "The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6563
    DOI: 10.1038/ncomms6563
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    Cited by:

    1. Elyse S. Fischer & Conny W. H. Yu & Johannes F. Hevler & Stephen H. McLaughlin & Sarah L. Maslen & Albert J. R. Heck & Stefan M. V. Freund & David Barford, 2022. "Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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