Rapid dephosphorylation of a Mr 80,000 protein, a specific substrate of protein kinase C upon removal of phorbol esters, bombesin and vasopressin.
The mitogens phorbol 12,13-dibutyrate, bombesin and vasopressin stimulate the phosphorylation of an acidic Mr 80,000 cellular protein, a specific substrate of protein kinase C, in intact Swiss 3T3 cells. Phosphorylation of this substrate was rapidly reversed upon the removal of each of these agents. Dephosphorylation occurred with a similar half-life in each of the cases studied (2.2, 1.5 and 2 minutes for phorbol 12,13-dibutyrate, bombesin and vasopressin respectively) and agreed closely with the dissociation of the ligands from their specific high-affinity binding sites in Swiss 3T3 cells.
Rodriguez-Pena
A
A
Zachary
I
I
Rozengurt
E
E
D001839:Bombesin / Q000494:pharmacology*; D002478:Cells, Cultured; D004075:Diglycerides / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D015240:Phorbol 12,13-Dibutyrate; D010703:Phorbol Esters / Q000494:pharmacology*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000032:analysis*; D014667:Vasopressins / Q000494:pharmacology*
D004075:Diglycerides; D010703:Phorbol Esters; D010750:Phosphoproteins; D014667:Vasopressins; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C; D001839:Bombesin