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

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Standard

The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing. / Lischetti, Tiziana; Zhang, Gang; Sedgwick, Garry G; Bolanos-Garcia, Victor M; Nilsson, Jakob.

I: Nature Communications, Bind 5, 5563, 12.2014, s. 1-12.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lischetti, T, Zhang, G, Sedgwick, GG, Bolanos-Garcia, VM & Nilsson, J 2014, 'The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing', Nature Communications, bind 5, 5563, s. 1-12. https://doi.org/10.1038/ncomms6563

APA

Lischetti, T., Zhang, G., Sedgwick, G. G., Bolanos-Garcia, V. M., & Nilsson, J. (2014). The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing. Nature Communications, 5, 1-12. [5563]. https://doi.org/10.1038/ncomms6563

Vancouver

Lischetti T, Zhang G, Sedgwick GG, Bolanos-Garcia VM, Nilsson J. The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing. Nature Communications. 2014 dec.;5:1-12. 5563. https://doi.org/10.1038/ncomms6563

Author

Lischetti, Tiziana ; Zhang, Gang ; Sedgwick, Garry G ; Bolanos-Garcia, Victor M ; Nilsson, Jakob. / The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing. I: Nature Communications. 2014 ; Bind 5. s. 1-12.

Bibtex

@article{39052f920f96448d8fbc0746b6c08cfe,
title = "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 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.",
author = "Tiziana Lischetti and Gang Zhang and Sedgwick, {Garry G} and Bolanos-Garcia, {Victor M} and Jakob Nilsson",
year = "2014",
month = dec,
doi = "10.1038/ncomms6563",
language = "English",
volume = "5",
pages = "1--12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - The internal Cdc20 binding site in BubR1 facilitates both spindle assembly checkpoint signalling and silencing

AU - Lischetti, Tiziana

AU - Zhang, Gang

AU - Sedgwick, Garry G

AU - Bolanos-Garcia, Victor M

AU - Nilsson, Jakob

PY - 2014/12

Y1 - 2014/12

N2 - 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.

AB - 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.

U2 - 10.1038/ncomms6563

DO - 10.1038/ncomms6563

M3 - Journal article

C2 - 25482201

VL - 5

SP - 1

EP - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 5563

ER -

ID: 128722841