We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
State of the APC/C: organization, function, and structure.
- Authors
McLean, Janel R; Chaix, Denis; Ohi, Melanie D; Gould, Kathleen L
- Abstract
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.
- Publication
Critical reviews in biochemistry and molecular biology, 2011, Vol 46, Issue 2, p118
- ISSN
1549-7798
- Publication type
Journal Article
- DOI
10.3109/10409238.2010.541420