The relationships between protein synthesis and neuronal survival are poorly understood. In chicken nucleus magnocellularis (NM), significant alterations in overall protein synthesis precede neuronal death induced by deprivation of excitatory afferent activity. Previously we demonstrated an initial reduction in the overall rate of protein synthesis in all deprived NM neurons,followed byquick recovery (starting at 6h) in some, but not all, neurons. Neurons with recovered protein synthesis ultimately survive while others become "ghost" cells (no detectable Nissl substance) at 12-24h and die within 48h. To explore the mechanisms underlying thisdifferentialinfluenceof afferent input on protein synthesis and cell survival, the current study investigates the involvement of eukaryotic translation elongation factor 2 (eEF2),the phosphorylation of which reduces overall protein synthesis. Using immunocytochemistry for either total or phosphorylated eEF2 (p-eEF2), we find significant reductions in the level of phosphorylated, but not total, eEF2 in NM neurons as early as 0.5h to 1h following cochlea removal. Unexpectedly, neurons with low levels of p-eEF2show reduced protein synthesis at 6h indicated by a marker for active ribosomes. At 12h, all "ghost" cellsexhibited little or no p-eEF2 staining although not every neuron with a comparable low level of p-eEF2 was a "ghost" cell. These observations demonstrate that areduced level of p-eEF2 is not responsible for immediate responses (including reduced overall protein synthesis) of a neuron to compromised afferent input, but may impair the neuron's ability toinitiate recovery signaling for survival and make the neuron more vulnerable to death. J. Comp. Neurol., 2012. © 2012 Wiley Periodicals, Inc.