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• W2034268892 endingPage "364" @default.
• W2034268892 startingPage "357" @default.
• W2034268892 abstract "Many proteins are targeted to proteasome degradation by a family of E3 ubiquitin ligases, termed SCF complexes, that link substrate proteins to an E2 ubiquitin-conjugating enzyme. SCFs are composed of three core proteins-Skp1, Cdc53/Cull, Rbx1/Hrt1-and a substrate specific F-box protein. We have identified in Drosophila melanogaster the closest homologues to the human components of the SCF(betaTrCP) complex and the E2 ubiquitin-conjugating enzyme UbcH5. We show that putative Drosophila SCF core subunits dSkpA and dRbx1 both interact directly with dCu11 and the F-box protein Slmb. We also describe the direct interaction of the UbcH5 related protein UbcD1 with dCul1 and Slmb. In addition, a functional complementation test performed on a Saccharomyces cerevisiae Hrt1p-deficient mutant showed that Drosophila Rbx1 is able to restore the yeast cells viability. Our results suggest that dRbx1, dSkpA, dCullin1, and Slimb proteins are components of a Drosophila SCF complex that functions in combination with the ubiquitin conjugating enzyme UbcD1." @default.
• W2034268892 created "2016-06-24" @default.
• W2034268892 creator A5000650663 @default.
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• W2034268892 date "2001-08-01" @default.
• W2034268892 modified "2023-09-23" @default.
• W2034268892 title "Occurrence of a Putative SCF Ubiquitin Ligase Complex in Drosophila" @default.
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• W2034268892 doi "https://doi.org/10.1006/bbrc.2001.5394" @default.
• W2034268892 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11500045" @default.
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