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- Title
Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation.
- Authors
Anabelle Decottignies; Aude Evain; Michel Ghislain
- Abstract
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, Cuil3p, 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 ubiquitinprotein fusions. The Cuil3 proteins were also found to interact with Ufd3p, a WD repeat protein known to associate with Cdc48p. Together, these results indicate that the Cuil3 proteins form complexes that are components of the ubiquitinproteasome system. Copyright © 2003 John Wiley & Sons, Ltd.
- Subjects
PROTEINS; MEMBRANE fusion; GENES; UBIQUITIN; ADENOSINE triphosphatase; BIODEGRADATION
- Publication
Yeast, 2004, Vol 21, Issue 2, p127
- ISSN
0749-503X
- Publication type
Article