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

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 cDN...

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Bibliographic Details
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
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.85.12.4538