CSP, an important neuroprotective DnaJ chaperone, is palmitoylated by Golgi-localized DHHC enzymes (DHHC3, DHHC7, DHHC15, and DHHC17; Greaves et al., 2008) . In this regard, CSP is similar to most other peripheral palmitoylated proteins. Consistent with the analyses of CSP palmitoylation in mammalian cells, disruption of DHHC17 in Drosophila melanogaster resulted in a loss of palmitoylation and mislocalization of CSP (Ohyama et al., 2007; Stowers and Isacoff, 2007) . Surprisingly, however, DHHC17 does not exhibit a Golgi localization in Drosophila neurons but, instead, has a presynaptic distribution on synaptic vesicles or at the presynaptic plasma membrane (Ohyama et al., 2007; Stowers and Isacoff, 2007) . Although palmitoylation cycles have not been reported for CSP, it is possible that DHHC17 is important for regulating local palmitoylation dynamics of CSP in Drosophila presynaptic terminals.