Harnessing the Ubiquitination Machinery to Target the Degradation of Specific Cellular Proteins
Open accessAbstract
The functional characterization of a specific gene, or its protein product, often relies on assessing the consequences of its elimination, usually accomplished by gene knockout, ribozyme, antisense, or RNA-mediated interference (RNAi) technologies. The selective degradation of cellular proteins is mediated primarily by the ubiquitin-proteasome pathway. Manipulation of the ubiquitin-dependent proteolytic machinery to eliminate specific gene products at the protein level has been previously attempted with some success in vitro; however, the in vivo efficacy of this approach has not yet been achieved. Here we report successful engineering of the substrate receptor of a major ubiquitin-proteolytic machinery to direct the degradation of otherwise stable cellular proteins both in yeast and in mammalian cells.
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Zhou et al. described some of the earliest chimeric bioPROTACs, including a fusion consisting of full-length β-TRCP protein and an N-terminal peptide of the E7 protein of HPV-16 that degraded retinoblastoma protein (RB1) in a human osteosarcoma cell line.
“Zhou et al.210 described some of the earliest chimeric bioPROTACs, including a fusion consisting of full-length β-TRCP protein and an N-terminal peptide of the E7 protein of human papillomavirus type 16 (HPV-16) that degraded retinoblastoma protein (RB1) in a human osteosarcoma cell line.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [210]
These studies demonstrated that the SCF E3 ligase could be redirected to degrade non-SCF targets.
“These studies demonstrated that the SCF E3 ligase could be redirected to degrade non-SCF targets.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [210]
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- Authors
- Zhou, P., Bogacki, R., McReynolds, L., & Howley, P. M.
- Affiliations
- Harvard University (US)
- Corresponding author
- Zhou, Pengbo
- Howley, Peter M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 6
- Issue
- 3
- Pages
- 751-756
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2034414781
- Cited by
- 164
- References
- 23
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 7 · 2023: 9 · 2022: 8 · 2021: 3 · 2020: 8 · 2019: 6 · 2018: 5 · 2017: 5 · 2016: 7 · 2015: 6 · 2014: 9 · 2013: 6 · 2012: 2
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA064888, R01-CA64888-06)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- ubiquitination, protein degradation, ubiquitin-proteasome system, selective protein degradation, proteasome, RNA interference, yeast, mammalian cells
- MeSH terms
- F-Box-WD Repeat-Containing Protein 7, Animals, Uterine Cervical Neoplasms, Female, Humans, Ligases, Mammals, Molecular Biology, Nuclear Proteins, Plasmids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Osteosarcoma, Substrate Specificity, Tumor Cells, Cultured, Ubiquitins, Gene Expression Regulation, Enzymologic, Retinoblastoma Protein, Cell Cycle Proteins, GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases, F-Box Proteins, beta-Transducin Repeat-Containing Proteins, Retinoblastoma-Like Protein p107
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