Mechanisms of Deubiquitinase Specificity and Regulation
Harvard University · MRC Laboratory of Molecular Biology · +1 more institution
Abstract
Protein ubiquitination is one of the most powerful posttranslational modifications of proteins, as it regulates a plethora of cellular processes in distinct manners. Simple monoubiquitination events coexist with more complex forms of polyubiquitination, the latter featuring many different chain architectures. Ubiquitin can be subjected to further posttranslational modifications (e.g., phosphorylation and acetylation) and can also be part of mixed polymers with ubiquitin-like modifiers such as SUMO (small ubiquitin-related modifier) or NEDD8 (neural precursor cell expressed, developmentally downregulated 8). Together, cellular ubiquitination events form a sophisticated and versatile ubiquitin code.…
Citation impact
- FWCI
- 33.08
- Percentile
- 100%
- References
- 197
Authors
2Topics & keywords
- Ubiquitin
- Deubiquitinating enzyme
- NEDD8
- SUMO enzymes
- Acetylation
- Biology
- Cell biology
- Ubiquitin ligase