promote stable membrane attachment of SNAP25 (Greaves et al., 2009a) . Recent work also reported that SNAP25 can be palmitoylated by DHHC2 but that this enzyme is unable to promote stable membrane attachment (Greaves et al., 2010) . This observation is consistent with the idea that palmitoylation of newly synthesized SNAP25 (which promotes membrane association) is restricted to the Golgi and that modification by post-Golgi DHHCs is only relevant once SNAP25 has been trafficked from Golgi to plasma membrane. This may reflect a weaker association between SNAP25 and DHHC2, such that productive interaction can only occur when SNAP25 is stably membrane associated. However, it is also consistent with the idea that unpalmitoylated SNAP25 may have a higher affinity for Golgi membranes than the plasma membrane, again reinforcing the importance of membrane affinities and preferences of peripheral proteins before palmitoylation (see previous paragraph).