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Vol. 16, No. 3, pp. 289-294, February 1, 2002
1 Section of Molecular Cell and Developmental Biology
and 2 Section of Neurobiology, Institute for Cellular and Molecular
Biology, The University of Texas at Austin, Austin, Texas 78712, USA
Eukaryotic genomes encode large families of deubiquitinating
enzymes (DUBs). Genetic data suggest that Fat facets (Faf), a Drosophila DUB essential for patterning the compound eye, might have a novel regulatory function; Faf might reverse the ubiquitination of a specific substrate, thereby preventing proteasomal degradation of
that protein. Additional genetic data implicate Liquid facets (Lqf), a
homolog of the vertebrate endocytic protein epsin, as a candidate for
the key substrate of Faf. Here, biochemical experiments critical to testing this model were performed. The results show definitively that Lqf is the key substrate of Faf in the eye; Lqf
concentration is Faf-dependent, Lqf is ubiquitinated in vivo and
deubiquitinated by Faf, and Lqf and Faf interact physically.
[Key Words: Fat facets; deubiquitinating enzyme; Liquid facets; epsin; eye development; endocytosis]
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