title: VAMP-1: a synaptic vesicle-associated integral membrane protein.
abstract: Several proteins are associated with, or are integral components of, the lipid bilayer that forms the delineating membrane of neuronal synaptic vesicles. To characterize these molecules, we used a polyclonal antiserum raised against purified cholinergic synaptic vesicles from Torpedo to screen a cDNA expression library constructed from mRNA of the electromotor nucleus. One clone encodes VAMP-1 (vesicle-associated membrane protein 1), a nervous-system-specific protein of 120 amino acids whose primary sequence can be divided into three domains: a proline-rich amino terminus, a highly charged internal region, and a hydrophobic carboxyl-terminal domain that is predicted to comprise a membrane anchor. Tryptic digestion of intact and lysed vesicles suggests that the protein faces the cytoplasm, where it may play a role in packaging, transport, or release of neurotransmitters.
authors: Department of Biological Sciences, Stanford University, CA 94305.
authors: W S
authors: WS
authors: Trimble
authors: D M
authors: DM
authors: Cowan
authors: R H
authors: RH
authors: Scheller
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004557:Electric Organ / Q000378:metabolism; D005796:Genes; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000235:genetics*; D050683:R-SNARE Proteins; D013572:Synaptic Vesicles / Q000378:metabolism* / Q000648:ultrastructure; D014101:Torpedo
chemical_list: D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins