CCDC68 Maintains Mitotic Checkpoint Activation by Promoting CDC20 Integration into the MCC

Author:

Li Qi1,Chen Qingzhou1,Zheng Tao1,Wang Fulin1,Teng Junlin1,Zhou Haining2,Chen Jianguo13ORCID

Affiliation:

1. Key Laboratory of Cell Proliferation and Differentiation of the Ministry of Education College of Life Sciences Peking University Beijing 100871 China

2. Key Laboratory of Epigenetic Regulation and Intervention Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China

3. Center for Quantitative Biology Peking University Beijing 100871 China

Abstract

AbstractThe spindle assembly checkpoint (SAC) ensures chromosome segregation fidelity by manipulating unattached kinetochore‐dependent assembly of the mitotic checkpoint complex (MCC). The MCC binds to and inhibits the anaphase promoting complex/cyclosome (APC/C) to postpone mitotic exit. However, the mechanism by which unattached kinetochores mediate MCC formation is not yet fully understood. Here, it is shown that CCDC68 is an outer kinetochore protein that preferentially localizes to unattached kinetochores. Furthermore, CCDC68 interacts with the SAC factor CDC20 to inhibit its autoubiquitination and MCC disassembly. Therefore, CCDC68 restrains APC/C activation to ensure a robust SAC and allow sufficient time for chromosome alignment, thus ensuring chromosomal stability. Hence, the study reveals that CCDC68 is required for CDC20‐dependent MCC stabilization to maintain mitotic checkpoint activation.

Funder

National Natural Science Foundation of China

Key Technologies Research and Development Program

Publisher

Wiley

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