Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
By B. Schulman, J. Harper. Nature reviews. Molecular cell biology, 2009
940 citations recorded by the source corpus.
Attachment of ubiquitin or ubiquitin-like proteins (known as UBLs) to their targets through multienzyme cascades is a central mechanism to modulate protein functions. This process is initiated by a family of mechanistically and structurally related E1 (or activating) enzymes. These activate UBLs through carboxy-terminal adenylation and thiol transfer, and coordinate the use of UBLs in specific downstream pathways by charging cognate E2 (or conjugating) enzymes, which then interact with the downstream ubiquitylation machinery to coordinate the modification of the target. A broad understanding of how E1 enzymes activate UBLs and how they selectively coordinate UBLs with downstream function has come from enzymatic, structural and genetic studies.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/44db31c41ab0845a121901fe8ca24a5709b8ef3b
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Citations in the corpus
- Insights in Post-Translational Modifications: Ubiquitin and SUMO (2022, background): “The main mechanistical difference is that RING E3s facilitate the direct transfer of ubiquitin from the E2 to the target protein, whilst HECT and RBR E3s contain an active site cysteine that forms a thioester bond with ubiquitin before transferring it to the substrate [7,48,49] (Figure 3).”
- Sumoylation: a regulatory protein modification in health and disease. (2013, background): “For details of the elaborate reaction mechanism that is shared by all E1 enzymes, the reader is referred to Reference 28 and two excellent reviews (29, 30).”