State of the APC/C: organization, function, and structure.

McLean JR, Chaix D, Ohi MD, Gould KL
Crit Rev Biochem Mol Biol. 2011 46 (2): 118-36

PMID: 21261459 · PMCID: PMC4856037 · DOI:10.3109/10409238.2010.541420

The ubiquitin-proteasome protein degradation system is involved in many essential cellular processes including cell cycle regulation, cell differentiation, and the unfolded protein response. The anaphase-promoting complex/cyclosome (APC/C), an evolutionarily conserved E3 ubiquitin ligase, was discovered 15 years ago because of its pivotal role in cyclin degradation and mitotic progression. Since then, we have learned that the APC/C is a very large, complex E3 ligase composed of 13 subunits, yielding a molecular machine of approximately 1 MDa. The intricate regulation of the APC/C is mediated by the Cdc20 family of activators, pseudosubstrate inhibitors, protein kinases and phosphatases and the spindle assembly checkpoint. The large size, complexity, and dynamic nature of the APC/C represent significant obstacles toward high-resolution structural techniques; however, over the last decade, there have been a number of lower resolution APC/C structures determined using single particle electron microscopy. These structures, when combined with data generated from numerous genetic and biochemical studies, have begun to shed light on how APC/C activity is regulated. Here, we discuss the most recent developments in the APC/C field concerning structure, substrate recognition, and catalysis.

MeSH Terms (13)

Anaphase-Promoting Complex-Cyclosome Animals Catalysis Cell Cycle Proteins Cell Nucleus Humans Meiosis Microscopy, Electron Mitosis Models, Biological Spindle Apparatus Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases

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