VAMP-1: A Synaptic Vesicle-Associated Integral Membrane Protein

• Published in: Proceedings of the National Academy of Sciences - PNAS 1988-06, Vol.85 (12), p.4538-4542
• Main Authors: Trimble, William S., Cowan, David M., Scheller, Richard H.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Antibodies; Antiserum; Base Sequence; Biological and medical sciences; Cell membranes; Cell physiology; Cloning, Molecular; Complementary DNA; Cytoplasm; Electric Organ - metabolism; Fundamental and applied biological sciences. Psychology; Gels; Genes; Membrane Proteins; Molecular and cellular biology; Molecular Sequence Data; Molecular Weight; Molecules; Nerve Tissue Proteins - genetics; Neurotransmission; P branes; R-SNARE Proteins; RNA; synaptic vesicles; Synaptic Vesicles - metabolism; Synaptic Vesicles - ultrastructure; Torpedo; Torpedo californica
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.85.12.4538

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.