期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 6, 页码 3457-3467出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.514430
关键词
Cell Cycle; Cyclins; Mitosis; Protein Degradation; Ubiquitin; APC; C; APPOLON; Cyclin A; Spindle Assembly Checkpoint
资金
- Ministry of Education, Science, Sports and Culture, Japan
- NOVARTIS Foundation (Japan) for the Promotion of Science
- Cosmetology Research Foundation
- Grants-in-Aid for Scientific Research [25112521, 23790117, 25460084] Funding Source: KAKEN
Background: CYCLIN A is degraded in early mitosis independent of spindle assembly checkpoint. Results: APOLLON interacts with CYCLIN A and promotes its degradation in mitosis. Conclusion: APOLLON is a novel regulator of CYCLIN A degradation in early mitosis. Significance: This study expands our knowledge on the huge APOLLON protein known to regulate apoptosis and cytokinesis. In the mammalian cell cycle, both CYCLIN A and CYCLIN B are required for entry into mitosis, and their elimination is also essential to complete the process. During mitosis, CYCLIN A and CYCLIN B are ubiquitylated by the anaphase-promoting complex/cyclosome (APC/C) and then subjected to proteasomal degradation. However, CYCLIN A, but not CYCLIN B, begins to be degraded in the prometaphase when APC/C is inactivated by the spindle assembly checkpoint (SAC). Here, we show that APOLLON (also known as BRUCE or BIRC6) plays a role in SAC-independent degradation of CYCLIN A in early mitosis. APPOLON interacts with CYCLIN A that is not associated with cyclin-dependent kinases. APPOLON also interacts with APC/C, and it facilitates CYCLIN A ubiquitylation. In APPOLON-deficient cells, mitotic degradation of CYCLIN A is delayed, and the total, but not the cyclin-dependent kinase-bound, CYCLIN A level was increased. We propose APPOLON to be a novel regulator of mitotic CYCLIN A degradation independent of SAC.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据