The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores

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The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores. / Zhang, Gang; Nilsson, Jakob.

In: Cell Cycle, Vol. 17, No. 9, 2018, p. 1087-1091.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Zhang, G & Nilsson, J 2018, 'The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores', Cell Cycle, vol. 17, no. 9, pp. 1087-1091. https://doi.org/10.1080/15384101.2018.1480209

APA

Zhang, G., & Nilsson, J. (2018). The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores. Cell Cycle, 17(9), 1087-1091. https://doi.org/10.1080/15384101.2018.1480209

Vancouver

Zhang G, Nilsson J. The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores. Cell Cycle. 2018;17(9):1087-1091. https://doi.org/10.1080/15384101.2018.1480209

Author

Zhang, Gang ; Nilsson, Jakob. / The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores. In: Cell Cycle. 2018 ; Vol. 17, No. 9. pp. 1087-1091.

Bibtex

@article{60a0126a916c4911a8df9a0653fac146,
title = "The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores",
abstract = "The spindle assembly checkpoint (SAC) ensures accurate chromosome segregation by delaying anaphase onset in response to unattached kinetochores. Anaphase is delayed by the generation of the mitotic checkpoint complex (MCC) composed of the checkpoint proteins Mad2 and BubR1/Bub3 bound to the protein Cdc20. Current models assume that MCC production is catalyzed at unattached kinetochores and that the Mad1/Mad2 complex is instrumental in the conversion of Mad2 from an open form (O-Mad2) to a closed form (C-Mad2) that can bind to Cdc20. Importantly the levels of Mad2 at kinetochores correlate with SAC activity but whether C-Mad2 at kinetochores exclusively represents its complex with Mad1 is not fully established. Here we use a recently established C-Mad2 specific monoclonal antibody to show that Cdc20 and C-Mad2 levels correlate at kinetochores and that depletion of Cdc20 reduces Mad2 but not Mad1 kinetochore levels. Importantly reintroducing wild type Cdc20 but not Cdc20 R132A, a mutant form that cannot bind Mad2, restores Mad2 levels. In agreement with this live cell imaging of fluorescent tagged Mad2 reveals that Cdc20 depletion strongly reduces Mad2 localization to kinetochores. These results support the presence of Mad2-Cdc20 complexes at kinetochores in agreement with current models of the SAC but also argue that Mad2 levels at kinetochores cannot be used as a direct readout of Mad1 levels.",
author = "Gang Zhang and Jakob Nilsson",
year = "2018",
doi = "10.1080/15384101.2018.1480209",
language = "English",
volume = "17",
pages = "1087--1091",
journal = "Cell Cycle",
issn = "1538-4101",
publisher = "Taylor & Francis",
number = "9",

}

RIS

TY - JOUR

T1 - The closed form of Mad2 is bound to Mad1 and Cdc20 at unattached kinetochores

AU - Zhang, Gang

AU - Nilsson, Jakob

PY - 2018

Y1 - 2018

N2 - The spindle assembly checkpoint (SAC) ensures accurate chromosome segregation by delaying anaphase onset in response to unattached kinetochores. Anaphase is delayed by the generation of the mitotic checkpoint complex (MCC) composed of the checkpoint proteins Mad2 and BubR1/Bub3 bound to the protein Cdc20. Current models assume that MCC production is catalyzed at unattached kinetochores and that the Mad1/Mad2 complex is instrumental in the conversion of Mad2 from an open form (O-Mad2) to a closed form (C-Mad2) that can bind to Cdc20. Importantly the levels of Mad2 at kinetochores correlate with SAC activity but whether C-Mad2 at kinetochores exclusively represents its complex with Mad1 is not fully established. Here we use a recently established C-Mad2 specific monoclonal antibody to show that Cdc20 and C-Mad2 levels correlate at kinetochores and that depletion of Cdc20 reduces Mad2 but not Mad1 kinetochore levels. Importantly reintroducing wild type Cdc20 but not Cdc20 R132A, a mutant form that cannot bind Mad2, restores Mad2 levels. In agreement with this live cell imaging of fluorescent tagged Mad2 reveals that Cdc20 depletion strongly reduces Mad2 localization to kinetochores. These results support the presence of Mad2-Cdc20 complexes at kinetochores in agreement with current models of the SAC but also argue that Mad2 levels at kinetochores cannot be used as a direct readout of Mad1 levels.

AB - The spindle assembly checkpoint (SAC) ensures accurate chromosome segregation by delaying anaphase onset in response to unattached kinetochores. Anaphase is delayed by the generation of the mitotic checkpoint complex (MCC) composed of the checkpoint proteins Mad2 and BubR1/Bub3 bound to the protein Cdc20. Current models assume that MCC production is catalyzed at unattached kinetochores and that the Mad1/Mad2 complex is instrumental in the conversion of Mad2 from an open form (O-Mad2) to a closed form (C-Mad2) that can bind to Cdc20. Importantly the levels of Mad2 at kinetochores correlate with SAC activity but whether C-Mad2 at kinetochores exclusively represents its complex with Mad1 is not fully established. Here we use a recently established C-Mad2 specific monoclonal antibody to show that Cdc20 and C-Mad2 levels correlate at kinetochores and that depletion of Cdc20 reduces Mad2 but not Mad1 kinetochore levels. Importantly reintroducing wild type Cdc20 but not Cdc20 R132A, a mutant form that cannot bind Mad2, restores Mad2 levels. In agreement with this live cell imaging of fluorescent tagged Mad2 reveals that Cdc20 depletion strongly reduces Mad2 localization to kinetochores. These results support the presence of Mad2-Cdc20 complexes at kinetochores in agreement with current models of the SAC but also argue that Mad2 levels at kinetochores cannot be used as a direct readout of Mad1 levels.

U2 - 10.1080/15384101.2018.1480209

DO - 10.1080/15384101.2018.1480209

M3 - Journal article

C2 - 29895228

VL - 17

SP - 1087

EP - 1091

JO - Cell Cycle

JF - Cell Cycle

SN - 1538-4101

IS - 9

ER -

ID: 198720419