Inhibition of 2'-phosphodiesterase by cAMP-dependent protein kinase. Involvement of phosphorylation of protein inhibitor.
2'-Phosphodiesterase from NIH 3T3 cells was purified about 530-fold. Treatment of the cell lysate with the cAMP-dependent protein kinase causing the 2'-phosphodiesterase inhibition did not result in phosphorylation of the enzyme itself. The kinase was found to phosphorylate a specific 18-kDa protein, the phosphorylated form of this protein being the inhibitor of 2'-phosphodiesterase.
D000818:Animals; D002460:Cell Line; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D000242:Cyclic AMP / Q000494:pharmacology*; D005095:Exoribonucleases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D051379:Mice; D010750:Phosphoproteins / Q000302:isolation & purification / Q000494:pharmacology*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*
D010750:Phosphoproteins; D000242:Cyclic AMP; D011494:Protein Kinases; D005095:Exoribonucleases; C029364:2'-phosphodiesterase