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

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

Authors

  • Huang Y
  • Baker RT
  • Fischer-Vize JA

Journal

Science (New York, N.Y.)

Publication Data

December 15, 1995

Associated Grants

None

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