The emerging complexity of protein ubiquitination
MRC Laboratory of Molecular Biology
Abstract
Protein ubiquitination and protein phosphorylation are two fundamental regulatory post-translational modifications controlling intracellular signalling events. However, the ubiquitin system is vastly more complex compared with phosphorylation. This is due to the ability of ubiquitin to form polymers, i.e. ubiquitin chains, of at least eight different linkages. The linkage type of the ubiquitin chain determines whether a modified protein is degraded by the proteasome or serves to attract proteins to initiate signalling cascades or be internalized. The present review focuses on the emerging complexity of the ubiquitin system. I review what is known about individual chain types, and highlight recent advances that…
Citation impact
- FWCI
- 23.68
- Percentile
- 100%
- References
- 154
Authors
1Topics & keywords
- Ubiquitin
- Phosphorylation
- Cell biology
- Proteasome
- Allosteric regulation
- F-box protein
- Deubiquitinating enzyme
- Signalling