Neurons are among the largest and most complex cells in nature, often extending very long axons, which in adult mammals, including humans, can reach up to one meter in length. These extraordinary morphological features pose a challenging problem as to how information codified in the nucleus can reach the periphery of the cell in a timely manner to respond to extrinsic stimuli. Similar to virtually all eukaryotic cells, neurons have adopted the strategy of localizing RNA asymmetrically. The nature of the transcripts targeted to dendrites and axons have been extensively studied, and they encode synaptic proteins, cytoskeleton components, ion channels, mitochondrial and ribosomal proteins, and proteins required for plasma membrane biogenesis. However, the mechanism underlying local translation has remained elusive. On page 1416 of this issue, Terenzio et al. add a new piece to the puzzle and show that local translation to produce the protein mammalian target of rapamycin (mTOR) precedes the burst of protein synthesis associated with the regeneration of injured axons. mTOR is a serine/threonine kinase that plays a central role in regulating protein synthesis.