The Ubiquitin Code

@article{Komander2012TheUC,
  title={The Ubiquitin Code},
  author={David Komander and Michael Rap{\'e}},
  journal={The Ubiquitin Code},
  year={2012}
}
The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells. Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct conformations and lead to different outcomes in cells. Here, we discuss the structure, assembly, and… 
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197 References

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Crystal structures of the Nedd4 HECT domain show a new binding mode involving two surfaces on ubiquitin and both subdomains of the HECT N‐lobe, which suggest a model for HECT‐to‐substrate ubiquitIn transfer, in which the growing chain on the substrate is kept close to the catalytic cysteine to promote processivity.

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A model for the interaction of diubiquitin and a ubiquitin conjugating enzyme (E2) is proposed and suggests determinants for recognition of multiubiquITin chains.

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