Harnessing the ubiquitination machinery to target the degradation of specific cellular proteins.

TitleHarnessing the ubiquitination machinery to target the degradation of specific cellular proteins.
Publication TypeJournal Article
Year of Publication2000
AuthorsZhou P, Bogacki R, McReynolds L, Howley PM
JournalMol Cell
Date Published2000 Sep
KeywordsAnimals, beta-Transducin Repeat-Containing Proteins, Cell Cycle Proteins, F-Box Proteins, F-Box-WD Repeat-Containing Protein 7, Female, Gene Expression Regulation, Enzymologic, GTP-Binding Proteins, Humans, Ligases, Mammals, Molecular Biology, Nuclear Proteins, Osteosarcoma, Plasmids, Recombinant Fusion Proteins, Retinoblastoma Protein, Retinoblastoma-Like Protein p107, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity, Tumor Cells, Cultured, Ubiquitin-Protein Ligases, Ubiquitins, Uterine Cervical Neoplasms

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.

Alternate JournalMol Cell
PubMed ID11030355
Grant ListR01-CA64888-06 / CA / NCI NIH HHS / United States
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Pengbo Zhou, Ph.D.

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