Article
Activation of an alpha2A-adrenoceptor-Galphao1 fusion protein dynamically regulates the palmitoylation status of the G protein but not of the receptor.
The Biochemical journal - 1 Jan 2005
Barclay Elaine, O'Reilly Mark, Milligan Graeme
Abstract excerpt
Post-translational thio-acylation of a fusion protein between the alpha2A-adrenoceptor and the alpha subunit of the G protein G(o1) is both dynamic and regulated by agonist binding. Incorporation of [3H]palmitate into the fusion protein was reduced substantially in the presence of the agonist adrenaline. This was dependent on the concentration of adrenaline and correlated with occupancy of the ligand binding...
Topics
- Acylation
- Cell Line
- Dose-Response Relationship, Drug
- Epinephrine
- GTP-Binding Protein alpha Subunits, Gi-Go
- Guanosine Triphosphate
- Humans
- Kinetics
- Ligands
- Mutation
- Palmitates
- Receptors, Adrenergic, alpha-2
- Recombinant Fusion Proteins