Priming and Extending: A UbcH5/Cdc34 E2 Handoff Mechanism for Polyubiquitination on a SCF Substrate
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We describe a mechanistic model of polyubiquitination by the SCF(beta TrCP2) E3 ubiquitin (Ub) ligase using human I kappaB alpha as a substrate. Biochemical reconstitution experiments revealed that the polyubiquitination of I kappaB alpha began with the action of the UbcH5 E2 Ub-conjugating enzyme, transferring a single Ub to I kappaB alpha K21/K22 rapidly and efficiently. Subsequently, the Cdc34 E2 functioned in the formation of polyubiquitin chains. It was determined that a Ub fused at I kappaB alpha K21 acts as a receptor, directing Cdc34 for rapid and efficient K48-linked Ub chain synthesis that depends on SCF(beta TrCP2) and the substrate's N terminus. The I kappaB alpha-linked fusion Ub appears to mediate direct contacts with Cdc34 and the SCF's RING subcomplex. Taken together, these results suggest a role for the multifaceted interactions between the I kappaB alpha K21/K22-linked receptor Ub, the SCF's RING complex, and Cdc34 approximately S approximately Ub in establishing the optimal orientation of the receptor Ub to drive conjugation.
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UBE2D knockdown stabilizes the CRL1β-TRCP substrate IκBα.
“UBE2D knockdown stabilizes the CRL1β-TRCP substrate IκBα21”
From NEDD8 nucleates a multivalent cullin–RING–UBE2D ubiquitin ligation assembly (2020) · cites this paper as [21]
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Self-citation
- Authors
- Wu, K., Kovacev, J., & Pan, Z.-Q.
- Affiliations
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Pan, Zhen-Qiang
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 37
- Issue
- 6
- Pages
- 784-796
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC2862584
- OpenAlex
- W2010517835
- Cited by
- 126
- References
- 30
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 15 · 2023: 5 · 2022: 6 · 2021: 11 · 2020: 9 · 2019: 8 · 2018: 4 · 2017: 3 · 2016: 9 · 2015: 7 · 2014: 10 · 2013: 6 · 2012: 7
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (CA 095634, R01CA095634)
- National Institute of General Medical Sciences (GM61051, R01GM061051)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- polyubiquitination, Cdc34, E2 ubiquitin-conjugating enzyme, E3 ubiquitin ligase, IκBα, ring complexes, ubiquitin receptors, NF-κB signaling
- MeSH terms
- Humans, Substrate Specificity, RNA, Small Interfering, Ubiquitin-Protein Ligase Complexes, Ubiquitin-Conjugating Enzymes, SKP Cullin F-Box Protein Ligases, Cell Line, Tumor, I-kappa B Kinase, Ubiquitination, Biocatalysis, Anaphase-Promoting Complex-Cyclosome
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