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bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA)
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Abstract
Significance: Intracellular proteins interact with each other to perform functions that are critical to normal and disease states. Attempts at altering pathological protein–protein interactions with traditional approaches have largely failed. Here, we explore an emerging approach we call “bioPROTACs”—engineered fusion proteins that consist of a target binding domain and an E3 ligase, an arrangement that results in the specific degradation of the therapeutic target. Our systematic study shows bioPROTAC design requirements are highly flexible in terms of both the binding domain and E3 ligase components. Resulting molecules can be used as powerful tools for uncovering biology, informing on the design of small molecule target degraders (e.g. PROTACs), and, if delivery issues can be addressed, potential therapeutics.
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“The platform has been used to generate GFP-degrading bioPROTACs based on various E3 ligases: the CUL1 ligases β-TRCP, F-box and WD repeat domain-containing 7 (FBW7) and SKP2; the CUL2 ligase VHL; the CUL3 ligase speckle type BTB/POZ protein (SPOP); the CUL5 ligases suppressor of cytokine signalling 2 (SOCS2) and ankyrin repeat and SOCS box-containing 1 (ASB1); and the U-box E3 ligase CHIP.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [214]
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Metadata
- Authors
- Lim, S., Khoo, R., Peh, K. M., Teo, J., Chang, S. C., Ng, S., Beilhartz, G. L., Melnyk, R. A., Johannes, C. W., Brown, C. J., Lane, D. P., Henry, B., & Partridge, A. W.
- Affiliations
- MSD (Singapore) (SG)
- Pacific Translational Biomarkers, MSD International, Singapore 138665;
- Hospital for Sick Children (CA)
- University of Toronto (CA)
- Agency for Science, Technology and Research (SG)
- Corresponding author
- Partridge, Anthony W.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2020-03-02
- Volume
- 117
- Issue
- 11
- Pages
- 5791-5800
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC7084165
- OpenAlex
- W3010201122
- Cited by
- 170
- References
- 52
- Citations by year
- 2026: 30 · 2025: 38 · 2024: 35 · 2023: 26 · 2022: 18 · 2021: 15 · 2020: 8
- FWCI
- 5.43
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- PROTACs, targeted protein degradation, proliferating cell nuclear antigen, DNA synthesis, cell cycle progression, oncology drug targets
- MeSH terms
- Binding Sites, Humans, Protein Binding, Recombinant Proteins, Protein Engineering, Proliferating Cell Nuclear Antigen, Ubiquitin-Protein Ligases, HEK293 Cells, Molecular Targeted Therapy, Proteolysis
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