Article
Cellular environment is important in controlling V-ATPase dissociation and its dependence on activity.
The Journal of biological chemistry - 24 Aug 2007
Qi Jie, Forgac Michael
Abstract excerpt
One mechanism of regulating V-ATPase activity in vivo involves reversible dissociation into its component V(1) and V(0) domains, which in yeast occurs in response to glucose depletion. V-ATPase complexes containing the Vph1p isoform of subunit a (VCC) are targeted to the vacuole, and Stv1p-containing complexes (SCC) are targeted to the Golgi. Overexpression of Stv1p results in mistargeting of SCC to the vacuole....
Topics
- Adenosine Triphosphatases
- Catalysis
- Enzyme Inhibitors
- Fungal Proteins
- Glucose
- Golgi Apparatus
- Macrolides
- Models, Biological
- Mutagenesis, Site-Directed
- Mutation
- Protein Isoforms