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Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene.

Science (New York, N.Y.) | Dec 15, 1995

Ubiquitin is a highly conserved polypeptide found in all eukaryotes. The major function of ubiquitin is to target proteins for complete or partial degradation by a multisubunit protein complex called the proteasome. Here, the Drosophila fat facets gene, which is required for the appropriate determination of particular cells in the fly eye, was shown to encode a ubiquitin-specific protease (Ubp), an enzyme that cleaves ubiquitin from ubiquitin-protein conjugates. The Fat facets protein (FAF) acts as a regulatory Ubp that prevents degradation of its substrate by the proteasome. Flies bearing fat facets gene mutations were used to show that a Ubp is cell type--and substrate-specific and a regulator of cell fate decisions in a multicellular organism.

Pubmed ID: 8525378 RIS Download

Mesh terms: Amino Acid Sequence | Animals | Base Sequence | Cell Differentiation | Cysteine | Drosophila | Endopeptidases | Escherichia coli | Eye | Molecular Sequence Data | Mutagenesis, Site-Directed | Oligodeoxyribonucleotides | Recombinant Fusion Proteins | Ubiquitins | beta-Galactosidase

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Mouse Genome Informatics (Data, Gene Annotation)

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