The Drosophila eag gene has been shown to regulate neuronal excitability, olfaction, associative learning and larval locomotion. Not all of the roles of this gene in these processes can be explained by its function as a voltage-gated potassium channel. In this study, we show that the eag gene is spliced in a PKA- and PKC-regulated manner to produce a protein lacking channel domains. This protein, in the context of activated PKA, can engage cellular signaling pathways that alter cell structure. Nuclear localization is necessary for C-terminal-mediated effects, which also require MAPK. The requirement for PKA/PKC activation in the synthesis and function of this novel protein suggests that it may couple membrane events to nuclear signaling to regulate neuronal function on long time scales.