The Cholinergic Synapse International Symposium Held in Berlin, Germany on 23-27 September 1990
Abstract
From morphological and electrophysiological data, performed proteinaceous channels have been implicated in the release of neurotransmitters from their vesicular stores, synaptic vesicles. We have characterized different synaptic proteins which qualify as potential components of such hypothesized 'synaptopore' or 'fusion pore' structures: (1) Synaptophysin is a major integral membrane protein of synaptic vesicles that shares its transmembrane topolgy and structural organization with connexins, the subunits of gap junction proteins. By crosslinking and reconstitution techniques we have demonstrated that native synaptophysin contains six identical subunits and forms channels upon reconstitution in planar lipid bilayers. This protein therefore may correspond to the to the vesicular portion of a putative fusion pore structure. (2) Synaptoporin is another member of the synaptophysin/connexin channel protein family that is localized in small synaptic vesicles. In situ hybridization shows that this protein is selectively expressed in a subset of central neurons. (JS)
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 27, 1990
- Accession Number
- ADA229449