Publication Date:
1988-11-18
Description:
The quaternary structure and functional properties of synaptophysin, a major integral membrane protein of small presynaptic vesicles, were investigated. Cross-linking and sedimentation studies indicate that synaptophysin is a hexameric homo-oligomer, which in electron micrographs exhibits structural features common to channel-forming proteins. On reconstitution into planar lipid bilayers, purified synaptophysin displays voltage-sensitive channel activity with an average conductance of about 150 picosiemens. Because specific channels and fusion pores have been implicated in vesicular uptake and release of secretory compounds, synaptophysin may have a role in these processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thomas, L -- Hartung, K -- Langosch, D -- Rehm, H -- Bamberg, E -- Franke, W W -- Betz, H -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1050-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2461586" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Connexins
;
Ion Channels/*ultrastructure
;
Macromolecular Substances
;
Membrane Potentials
;
Membrane Proteins/physiology/*ultrastructure
;
Microscopy, Electron
;
Proteolipids
;
Synaptic Vesicles/physiology/*ultrastructure
;
Synaptophysin
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
