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* To whom correspondence should be addressed. E-mail: sdryer{at}uh.edu.
The protein kinase Akt is a crucial regulator of neuronal survival and apoptosis. Here we show that Akt activation is necessary for mobilization of large-conductance KCa channels in ciliary ganglion (CG) neurons evoked by 
-neuregulin-1 (NRG1) and TGF1. Application of NRG1 to embryonic day 9 (E9) CG neurons increased Akt phosphorylation, as observed previously for TGF1. NRG1- and TGF1-evoked stimulation of KCa is blocked by inhibitors of PI3K, by over-expression of a dominant-negative form of Akt, by over-expression of CTMP, an endogenous negative regulator of Akt, and by application of the Akt inhibitor 1L-6-hydroxymethyl-chiro-inositol 2-(R)-2-O-methyl-3-O-octadecylcarbonate (HIMO). Conversely, over-expression of a constitutively-active form of Akt was sufficient by itself to increase mobilization of functional KCa channels. NRG1 and TGF1 evoked an Akt-dependent increase in cell-surface SLO 
-subunits. These procedures have no effect on voltage-activated Ca2+ currents. Thus, Akt plays an essential role in the developmental regulation of excitability in CG neurons.
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