Article
Identification of an Hsp90 mutation that selectively disrupts cAMP/PKA signaling in Saccharomyces cerevisiae.
Current genetics - 1 Jun 2012
Flom Gary A, Langner Ewa, Johnson Jill L
Abstract excerpt
The molecular chaperone Hsp90 cooperates with multiple cochaperone proteins as it promotes the folding and activation of diverse client proteins. Some cochaperones regulate the ATPase activity of Hsp90, while others appear to promote Hsp90 interaction with specific types of client proteins. Through its interaction with the adenylate cyclase Cyr1, the Sgt1 cochaperone modulates the activity of the cAMP pathway in...
Topics
- Adaptor Proteins, Signal Transducing
- Amino Acid Sequence
- Antifungal Agents
- Cyclic AMP
- Cyclic AMP-Dependent Protein Kinases
- Gene Expression Regulation, Fungal
- HSP90 Heat-Shock Proteins
- Macrolides
- Molecular Sequence Data
- Morphogenesis
- Mutation
- Protein Binding
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Signal Transduction
- Transcription, Genetic
- Up-Regulation