title: Cysteine-string proteins: a cycle of acylation and deacylation?
abstract: 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.
authors.affiliation: Department of Molecular and Medical Pharmacology, UCLA School of Medicine 90095, USA.
authors.forename: C B
authors.initials: CB
authors.lastname: Gundersen
authors.forename: J A
authors.initials: JA
authors.lastname: Umbach
authors.forename: A
authors.initials: A
authors.lastname: Mastrogiacomo
mesh_terms: D000215:Acylation; D000818:Animals; D004331:Drosophila melanogaster / Q000196:embryology; D004705:Endocytosis; D005089:Exocytosis; D050956:HSP40 Heat-Shock Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D050956:HSP40 Heat-Shock Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D011500:Protein Synthesis Inhibitors; C088460:cysteine string protein; D014415:Tunicamycin