End-Binding E3 Ubiquitin Ligases Enable Protease Signaling Article Swipe
YOU?
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· 2019
· Open Access
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· DOI: https://doi.org/10.1021/acschembio.9b00621
Post-translational modifications (PTMs) direct the assembly of protein complexes. In this context, proteolysis is a unique PTM because it is irreversible; the hydrolysis of the peptide backbone generates separate fragments bearing a new N and C terminus. Proteolysis can "re-wire" protein-protein interactions (PPIs) via the recruitment of end-binding proteins to new termini. In this review, we focus on the role of proteolysis in specifically creating complexes by recruiting E3 ubiquitin ligases to new N and C termini. These complexes potentiate proteolytic signaling by "erasing" proteolytic modifications. This activity tunes the duration and magnitude of protease signaling events. Recent work has shown that the stepwise process of proteolysis, end-binding by E3 ubiquitin ligases, and fragment turnover is associated with both the nascent N terminus (i.e., N-degron pathways) and the nascent C terminus (i.e., the C-degron pathways). Here, we discuss how these pathways might harmonize protease signaling with protein homeostasis (i.e., proteostasis).
Related Topics
- Type
- review
- Language
- en
- Landing Page
- https://doi.org/10.1021/acschembio.9b00621
- OA Status
- green
- Cited By
- 8
- References
- 70
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2989125640
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2989125640Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1021/acschembio.9b00621Digital Object Identifier
- Title
-
End-Binding E3 Ubiquitin Ligases Enable Protease SignalingWork title
- Type
-
reviewOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2019Year of publication
- Publication date
-
2019-11-12Full publication date if available
- Authors
-
Matthew Ravalin, Koli Basu, Jason E. Gestwicki, Charles S. CraikList of authors in order
- Landing page
-
https://doi.org/10.1021/acschembio.9b00621Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
-
https://www.ncbi.nlm.nih.gov/pmc/articles/7400744Direct OA link when available
- Concepts
-
Ubiquitin, Ubiquitin-Protein Ligases, Protease, Ubiquitin ligase, Cell biology, Chemistry, Biochemistry, Biology, Computational biology, Enzyme, GeneTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
8Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 1, 2024: 2, 2022: 2, 2021: 2, 2020: 1Per-year citation counts (last 5 years)
- References (count)
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70Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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