The APC/C recruits cyclin B1-Cdk1-Cks in prometaphase before D box recognition to control mitotic exit
العنوان: | The APC/C recruits cyclin B1-Cdk1-Cks in prometaphase before D box recognition to control mitotic exit |
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المؤلفون: | Rob M. F. Wolthuis, Wouter van Zon, Hein te Riele, Janneke Ogink, Bas ter Riet, René H. Medema |
المصدر: | The Journal of Cell Biology |
سنة النشر: | 2010 |
مصطلحات موضوعية: | Prometaphase, Cyclin E, Cdc20 Proteins, Cyclin D, Recombinant Fusion Proteins, Cyclin A, Cyclin B, Mitosis, Cell Cycle Proteins, Anaphase-Promoting Complex-Cyclosome, Article, APC/C activator protein CDH1, Cell Line, CDC2 Protein Kinase, CDC2-CDC28 Kinases, Roscovitine, Animals, Humans, Cyclin B1, Phosphorylation, Protein Kinase Inhibitors, Research Articles, biology, Ubiquitin, Nocodazole, Ubiquitin-Protein Ligase Complexes, Cell Biology, Molecular biology, Cyclin-Dependent Kinases, Tubulin Modulators, Cell biology, Neoplasm Proteins, Securin, Purines, biology.protein, RNA Interference, Anaphase-promoting complex, Carrier Proteins, Cyclin A2, Protein Binding |
الوصف: | Prior associations with the APC/C complex during prometaphase makes cyclin B1 a better substrate for the cell cycle–regulating ubiquitin ligase in metaphase (see also a related paper by Di Fiore et al. in this issue). The ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C) is activated at prometaphase by mitotic phosphorylation and binding of its activator, Cdc20. This initiates cyclin A degradation, whereas cyclin B1 is stabilized by the spindle checkpoint. Upon checkpoint release, the RXXL destruction box (D box) was proposed to direct cyclin B1 to core APC/C or Cdc20. In this study, we report that endogenous cyclin B1–Cdk1 is recruited to checkpoint-inhibited, phosphorylated APC/C in prometaphase independently of Cdc20 or the cyclin B1 D box. Like cyclin A, cyclin B1 binds the APC/C by the Cdk cofactor Cks and the APC3 subunit. Prior binding to APC/CCdc20 makes cyclin B1 a better APC/C substrate in metaphase, driving mitotic exit and cytokinesis. We conclude that in prometaphase, the phosphorylated APC/C can recruit both cyclin A and cyclin B1 in a Cks-dependent manner. This suggests that the spindle checkpoint blocks D box recognition of APC/C-bound cyclin B1, whereas distinctive complexes between the N terminus of cyclin A and Cdc20 evade checkpoint control. |
تدمد: | 1540-8140 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41b36d76bfd940736505039b0319e85b https://pubmed.ncbi.nlm.nih.gov/20733055 |
حقوق: | OPEN |
رقم الأكسشن: | edsair.doi.dedup.....41b36d76bfd940736505039b0319e85b |
قاعدة البيانات: | OpenAIRE |
تدمد: | 15408140 |
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