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Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways

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Schulman, Brenda A., Wade Harper, J.·2009·Nature Reviews Molecular Cell Biology

Abstract

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.

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Metadata

Authors
Schulman, B. A., & Wade Harper, J.
Venue
Nature Reviews Molecular Cell Biology
Published
2009-04-08
Volume
10
Issue
5
Pages
319-331
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W1991841644
Cited by
943
References
4
FWCI
2.42
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. https://app.cochat.ai/papers/10.1038/nrm2673
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Schulman, B. A., & Wade Harper, J. (2009). Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm2673

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.