Involvement of protein kinase(s) in the intracellular signal transduction pathways for activation and adaptation of adenylate cyclase in Dictyostelium discoideum.
Binding of cyclic AMP (cAMP) to cell surface receptors induces activation and adaptation of adenylate cyclase while 2,3-dimercapto-1-propanol (BAL) acts only on the activation pathway. Here we show that an inhibitor of protein kinase (K252a) inhibits the cAMP-induced activation of the cyclase but not (rather enhances) the BAL-induced activation. These results suggest that protein kinase is involved in transduction of the activation signal and that phosphorylation might take place between the receptor and the action site of BAL. Since adaptation causes cessation of the activation, the enhancement of the BAL-induced cAMP accumulation by K252a might imply that K252a also blocks transduction of the adaptation signal.
Oyama
M
M
Department of Botany, Faculty of Science, Kyoto University, Japan.
Kubota
K
K
Okamoto
K
K
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D004023:Dictyostelium / Q000201:enzymology*; D004789:Enzyme Activation; D007700:Kinetics; D008954:Models, Biological; D011335:Proadifen / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D015398:Signal Transduction
D011335:Proadifen; D000242:Cyclic AMP; D011494:Protein Kinases; D000262:Adenylyl Cyclases