reviewBiochemical Society TransactionsSep 21, 2009Closed access

The emerging complexity of protein ubiquitination

MRC Laboratory of Molecular Biology

PubMed
Indexed incrossrefpubmed

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…

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Authors

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Topics & keywords

Keywords
  • Ubiquitin
  • Phosphorylation
  • Cell biology
  • Proteasome
  • Allosteric regulation
  • F-box protein
  • Deubiquitinating enzyme
  • Signalling
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