A viral K-RAS protein increases the stimulability of adenylate cyclase by cholera toxin in NRK cells

Abstract

Incubation at 41°C stops the proliferation of ts K-NRK rat kidney cells in serum-deficient medium by inactivating the mitogenic/oncogenic thermolabile viral K-RAS protein that is produced in these cells. Dropping the temperature to 36°C reactivates the viral K-RAS protein which stimulates the serum-starved quiescent cells to resume proliferating without added serum factors. Here it is shown that while the reactivated viral protein does not by itself significantly stimulate adenylate cyclase, it greatly increases the stimulability of adenylate cyclase by cholera toxin. The data suggest that the viral K-RAS protein directly or indirectly affects adenylate cyclase by inactivating the Gi inhibitory component of the membrane associated enzyme.