期刊
CELL CYCLE
卷 8, 期 1, 页码 167-171出版社
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.8.1.7606
关键词
Cdc20; spindle checkpoint; APC/C; Mad2; mitosis
类别
资金
- American Cancer Society
- NIH [5T32HL007151-30, R01-GM057587, R37-CA076584]
- NATIONAL CANCER INSTITUTE [R37CA076584] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [T32HL007151] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM057587] Funding Source: NIH RePORTER
The spindle assembly checkpoint (SAC) is an important mechanism that prevents the separation of sister chromatids until the microtubules radiating from the spindle poles are correctly attached to the kinetochores. Cdc20, an activator of the Anaphase Promoting Complex/Cyclosome (APC/C), is known as a major downstream target for inhibition by the SAC through the binding of mitotic checkpoint proteins, such as Mad2 and BubR1. Here, we report that the SAC negatively regulates the stability of Cdc20 by targeting it for proteasome-dependent degradation. Once the checkpoint is activated by spindle poisons, a major population of Cdc20 is degraded via APC/C, an event that requires the binding of Cdc20 to Mad2. We propose that the degradation of Cdc20 represents a critical control mechanism to ensure inactivation of APC/C-Cdc20 in response to the SAC.
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