Abstract
Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality control and degradation pathways. A huge range of ubiquitin signals can be generated depending on the specificity and catalytic activity of the enzymes required for attachment of ubiquitin to a given target. As a consequence of its importance to eukaryotic life, dysfunction in the ubiquitin system leads to many disease states, including cancers and neurodegeneration. This review takes a retrospective look at our progress in understanding the molecular mechanisms that govern the specificity of ubiquitin conjugation.
| Original language | English |
|---|---|
| Pages (from-to) | 212-227 |
| Number of pages | 16 |
| Journal | Biochemical Society Transactions |
| Volume | 44 |
| Issue number | 1 |
| Early online date | 9 Feb 2016 |
| DOIs | |
| Publication status | Published - 15 Feb 2016 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- ubiquitin
- E3 ligase
- RING
- RBR
- Fanconi anemia
- parkin
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