Abstract
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.
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Dates
Type | When |
---|---|
Created | 18 years, 9 months ago (Oct. 27, 2006, 2:19 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 12, 2024, 4:33 p.m.) |
Indexed | 1 month, 2 weeks ago (July 7, 2025, 2:28 a.m.) |
Issued | 29 years, 8 months ago (Dec. 15, 1995) |
Published | 29 years, 8 months ago (Dec. 15, 1995) |
Published Print | 29 years, 8 months ago (Dec. 15, 1995) |
@article{Huang_1995, title={Control of Cell Fate by a Deubiquitinating Enzyme Encoded by the fat facets Gene}, volume={270}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.270.5243.1828}, DOI={10.1126/science.270.5243.1828}, number={5243}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Huang, Yongzhao and Baker, Rohan T. and Fischer-Vize, Janice A.}, year={1995}, month=dec, pages={1828–1831} }