Article
Increased mitogenic responsiveness of Swiss 3T3 cells expressing constitutively active Gs alpha.
Biochemical and biophysical research communications - 16 May 1990
Zachary I, Masters S B, Bourne H R
Abstract excerpt
Mutational replacement of glutamine-227 with a leucine residue in the GTP-binding domain of the alpha subunit of GS (Q227L alpha S) reduces its ability to hydrolyse GTP and causes constitutive activation of the mutant protein. Expression in Swiss 3T3 fibroblasts of Q227L alpha S caused markedly increased basal adenylyl cyclase activity, enhanced intracellular cyclic AMP (cAMP) accumulation and increased mitogenic...
Topics
- Adenylyl Cyclases
- Amino Acid Sequence
- Animals
- Cell Line
- Cell Membrane
- Cell Transformation, Neoplastic
- Cyclic AMP
- Enzyme Activation
- GTP-Binding Proteins
- Glutamine
- Guanosine 5'-O-(3-Thiotriphosphate)
