Activating mutations in the NH2- and COOH-terminal moieties of the Gs alpha subunit have dominant phenotypes and distinguishable kinetics of adenylyl cyclase stimulation.

doi:10.1002/jcb.240470410

Article

Activating mutations in the NH2- and COOH-terminal moieties of the Gs alpha subunit have dominant phenotypes and distinguishable kinetics of adenylyl cyclase stimulation.

Journal of cellular biochemistry - 1 Dec 1991

Gupta S K, Dhanasekaran N, Heasley L E, Johnson G L

Abstract excerpt

The alpha subunit polypeptides of the G proteins Gs and Gi2 stimulate and inhibit adenylyl cyclase, respectively. The alpha s and alpha i2 subunits are 65% homologous in amino acid sequence but have highly conserved GDP/GTP binding domains. Previously, we mapped the functional adenylyl cyclase ac...

Topics

Adenylyl Cyclases
Animals
CHO Cells
Cell Membrane
Chimera
Cricetinae
Cyclic AMP
Enzyme Activation
Guanosine Diphosphate
Guanosine Triphosphate
Mutation
Phenotype

Activating mutations in the NH2- and COOH-terminal moieties of the Gs alpha subunit have dominant phenotypes and distinguishable kinetics of adenylyl cyclase stimulation.

Abstract excerpt

Topics

Discuss the evidence