Acute changes in cAMP and protein kinase A (PKA) signaling can regulate ion channel protein activities such as gating. Effects on channels due to chronic PKA signaling, as in stress or disease states, are less well understood. We examined the effects of prolonged PKA activity on the HERG K⁺ channel in stably transfected HEK cells. Sustained elevation of cAMP by either CPT-cAMP or forskolin increased the HERG channel protein abundance 2-4-fold within 24 hours, with measurable difference as early as four hours. The cAMP-induced augmentation was not due to changes in transcription and was specific for HERG compared to other cardiac K⁺ channels (Kv1.4, Kv1.5, Kir2.1 and KvLQT1). PKA activity was necessary for the effect on HERG protein and did not involve other cAMP signaling pathways. Direct PKA phosphorylation of the HERG protein was responsible for the cAMP-induced augmentation. Enhanced abundance of HERG protein was detected in ER, Golgi and plasma membrane without significant changes in trafficking rates or patterns. K⁺ An increase in current density carried by the HERG channel was also observed, but with a delay suggesting that traffic to the surface is rate-limiting traffic. Acceleration of the HERG protein synthesis rate was the primary factor in the cAMP/PKA effect with lesser effects on protein stability. These results provide evidence for a novel mechanism whereby phosphorylation of a nascent protein dictates its rate of synthesis, resetting its steady state abundance.