Cyclic AMP stimulates dephosphorylation of specific proteins in intact S49 mouse lymphoma cells.
Two-dimensional gel electrophoresis of proteins labeled with 32Pi in S49 mouse lymphoma cells revealed five phosphoproteins that were rapidly and reversibly dephosphorylated in response to elevation of cyclic AMP (cAMP). Under basal conditions, labeling of at least two of these proteins was limited by slow turnover of protein-bound phosphate. The rapid cAMP-mediated dephosphorylation of these species was attributable, therefore, to stimulation of a specific phosphoprotein phosphatase.
Kiss
Z
Z
Steinberg
R A
RA
D000818:Animals; D002460:Cell Line; D000242:Cyclic AMP / Q000494:pharmacology*; D007545:Isoproterenol / Q000494:pharmacology; D008223:Lymphoma / Q000378:metabolism*; D051379:Mice; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D013997:Time Factors
D010750:Phosphoproteins; D000242:Cyclic AMP; D010749:Phosphoprotein Phosphatases; D007545:Isoproterenol