A viral K-RAS protein increases the stimulability of adenylate cyclase by cholera toxin in NRK cells.
Incubation at 41 degrees C stops the proliferation of tsK-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 degrees 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.
D015056:1-Methyl-3-isobutylxanthine / Q000494:pharmacology; D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002455:Cell Division; D002460:Cell Line; D002772:Cholera Toxin / Q000494:pharmacology*; D000242:Cyclic AMP / Q000096:biosynthesis; D004247:DNA / Q000096:biosynthesis; D006358:Hot Temperature; D007668:Kidney / Q000166:cytology / Q000201:enzymology*; D009154:Mutation; D015689:Oncogene Protein p21(ras); D009856:Oncogene Proteins, Viral / Q000494:pharmacology*; D051381:Rats
D009856:Oncogene Proteins, Viral; D004247:DNA; D002772:Cholera Toxin; D000242:Cyclic AMP; D015689:Oncogene Protein p21(ras); D000262:Adenylyl Cyclases; D015056:1-Methyl-3-isobutylxanthine