Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 11, Pages 924-937Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2016.08.003
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Funding
- Rutherford Discovery Fellowship from the New Zealand government
- University of Otago
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Covalent modification of substrate proteins with ubiquitin is the end result of an intricate network of protein-protein interactions. The inherent ability of the E1, E2, and E3 proteins of the ubiquitylation cascade (the ubiquitin writers) to interact with ubiquitin facilitates this process. Importantly, contact between ubiquitin and the E2/E3 writers is required for catalysis and the assembly of chains of a given linkage. However, ubiquitin is also an activator of ubiquitin-writing enzymes, with many recent studies highlighting the ability of ubiquitin to regulate activity and substrate modification. Here, we review the interactions between ubiquitin-writing enzymes and regulatory ubiquitin molecules that promote activity, and highlight the potential of these interactions to promote processive ubiquitin transfer.
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