Cysteine-string proteins: a cycle of acylation and deacylation?

We used tunicamycin, an inhibitor of protein fatty acylation, to examine the possibility that there is a cycle of acylation and deacylation of cysteine string proteins at nerve terminals. Using both physiological and immunoblot approaches, we obtained no evidence for a cycle of acylation and deacylation that affects these proteins. These data suggest that this lipid modification of cysteine string proteins is relatively more stable than that observed for other nerve ending proteins, like SNAP-25.