Cited by 152Ubiquitin and proteasome pathwaysEnzyme Structure and FunctionProtein Degradation and Inhibitors

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NEDD8 and ubiquitin ligation by cullin-RING E3 ligases

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Baek, Kheewoong, Scott, Daniel C, Schulman, Brenda A·2021·Current Opinion in Structural Biology

DOI 10.1016/j.sbi.2020.10.007PMC PMC8096640

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Abstract

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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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
ORCID: Baek, Kheewoong
Scott, Daniel C
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)
DOI: 10.1016/j.sbi.2020.10.007
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: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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NEDD8 and ubiquitin ligation by cullin-RING E3 ligases

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