Noncovalent Ubiquitin Interactions Regulate the Catalytic Activity of Ubiquitin Writers.
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.
Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand; The Francis Crick Institute, London NW1 1AT, UK.
Joshua D
JD
Wright
Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand.
Peter D
PD
Mace
Department of Biochemistry, University of Otago, Dunedin 9054, New Zealand. Electronic address: catherine.day@otago.ac.nz.
Catherine L
CL
Day
D001665:Binding Sites; D055162:Biocatalysis; D005057:Eukaryotic Cells / Q000166:cytology / Q000378:metabolism*; D015870:Gene Expression; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D062105:Molecular Docking Simulation; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D013379:Substrate Specificity; D025801:Ubiquitin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D007527:Isoenzymes; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases
E2-conjugating enzyme; E3 ligase; ubiquitin