Specificity and disease in the ubiquitin system

Viduth K. Chaugule, Helen Walden (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)
195 Downloads (Pure)


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 languageEnglish
Pages (from-to)212-227
Number of pages16
JournalBiochemical Society Transactions
Issue number1
Early online date9 Feb 2016
Publication statusPublished - 15 Feb 2016


  • ubiquitin
  • E3 ligase
  • RING
  • RBR
  • Fanconi anemia
  • parkin


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