title: Cysteine-string proteins as templates for membrane fusion: models of synaptic vesicle exocytosis.
abstract: Cysteine-string proteins are relatively small, cysteine-rich components of synaptic vesicle membranes. Recent investigations demonstrated that at least 11 of the 13 cysteine residues of the Torpedo cysteine-string protein are fatty acylated. This exceptional level of fatty acylation occurs along a short stretch (less than 25 residues) of amino acids which are flanked on either side by very polar amino and carboxy termini. This amphipathic structure may have unique capabilities to catalyze events at membrane interfaces. We propose two distinct pathways to explain how these capabilities might subserve membrane fusion and exocytosis.
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: A
authors.initials: A
authors.lastname: Mastrogiacomo
authors.forename: J A
authors.initials: JA
authors.lastname: Umbach
mesh_terms: D000818:Animals; D005089:Exocytosis / Q000502:physiology*; D050956:HSP40 Heat-Shock Proteins; D008561:Membrane Fusion; D008565:Membrane Proteins; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D013572:Synaptic Vesicles / Q000502:physiology*
chemical_list: D050956:HSP40 Heat-Shock Proteins; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; C088460:cysteine string protein