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Science 18 November 1988:
Vol. 242. no. 4881, pp. 1050 - 1053
DOI: 10.1126/science.2461586
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Articles

Science, Vol 242, Issue 4881, 1050-1053
Copyright © 1988 by American Association for the Advancement of Science

articles

Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane

L Thomas, K Hartung, D Langosch, H Rehm, E Bamberg, WW Franke, and H Betz

Zentrum fur Molekulare Biologie, Universitat Heidelberg, Federal Republic of Germany.

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.


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