Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation.
The Cdc48/p97 AAA-ATPase functions in membrane fusion and ubiquitin-dependent protein degradation. Here, we show that, in yeast, Cdc48p interacts with three novel proteins, Cuil-3p, which contain a conserved ubiquitin-related (UBX) domain. Cui2p and Cui3p are closely related, interact with each other, and are localized at the perinuclear membrane. Cdc48p binds ... directly the UBX domain of Cui3p in vitro. Multiple deletions of the CUI1, CUI2 and CUI3 genes confer deficiency in sporulation and degradation of model ubiquitin-protein fusions. The Cuil-3 proteins were also found to interact with Ufd3p, a WD repeat protein known to associate with Cdc48p. Together, these results indicate that the Cuil-3 proteins form complexes that are components of the ubiquitin-proteasome system.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Amino Acid Sequence, Base Sequence, Carrier Proteins, Cell Cycle Proteins, DNA, Fungal, Membrane Proteins, Molecular Chaperones, Molecular Sequence Data, Mutagenesis, Insertional, Polymerase Chain Reaction, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Two-Hybrid System Techniques, Ubiquitin
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Amino Acid Sequence, Base Sequence, Carrier Proteins, Cell Cycle Proteins, DNA, Fungal, Membrane Proteins, Molecular Chaperones, Molecular Sequence Data, Mutagenesis, Insertional, Polymerase Chain Reaction, Protein Binding, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Two-Hybrid System Techniques, Ubiquitin
Yeast
Date: Jan. 30, 2004
PubMed ID: 14755638
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