NEDD8 and ubiquitin ligation by cullin-RING E3 ligases
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RING E3s comprise the largest family of ubiquitin (UB) and ubiquitin-like protein (UBL) ligases. RING E3s typically promote UB or UBL transfer from the active site of an associated E2 enzyme to a distally-recruited substrate. Many RING E3s - including the cullin-RING ligase family - are multifunctional, interacting with various E2s (or other E3s) to target distinct proteins, transfer different UBLs, or to initially modify substrates with UB or subsequently elongate UB chains. Here we consider recent structures of cullin-RING ligases, and their partner E2 enzymes, representing ligation reactions. The studies collectively reveal multimodal mechanisms - interactions between ancillary E2 or E3 domains, post-translational modifications, or auxiliary binding partners - directing cullin-RING E3-E2 enzyme active sites to modify their specific targets.
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Ubiquitin E3 ligases serve as scaffolds between a target protein and an activated E2-Ub, binding both and catalysing transfer of ubiquitin from the E2 active site cysteine to a lysine on the target.
“ubiquitin E3 ligases serve as scaffolds between a target protein and an activated ubiquitin E2 conjugating enzyme charged with a ubiquitin molecule (E2–Ub), by binding both molecules, then catalysing the transfer of ubiquitin from the active site cysteine of the E2 onto a lysine side chain of a target protein104–107.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [107]
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- Authors
- Baek, K., Scott, D. C., & Schulman, B. A.
- Affiliations
- Max Planck Institute of Biochemistry (DE)
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Schulman, Brenda A
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2021-04
- Volume
- 67
- Pages
- 101-109
- ISSN
- 0959-440X (ISSN-L)
- PMC
- PMC8096640
- OpenAlex
- W3096018906
- Cited by
- 152
- References
- 50
- Citations by year
- 2026: 21 · 2025: 21 · 2024: 34 · 2023: 28 · 2022: 33 · 2021: 15
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Current Opinion in Structural Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R01CA247365, P30CA021765)
- European Research Council (789016-NEDD8Activate)
- Deutsche Forschungsgemeinschaft (SCHU 3196/1-1)
- American Lebanese Syrian Associated Charities
- Horizon 2020
- Max-Planck-Gesellschaft
- St. Jude Children's Research Hospital
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- NEDD8, Cullin-RING E3 ligases, ubiquitin-like proteins, ubiquitination, post-translational modification, ubiquitin chain elongation
- MeSH terms
- Ubiquitins, Catalytic Domain, Ubiquitin, Ubiquitin-Protein Ligases, Cullin Proteins, Ubiquitination
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