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

  • Leo Thomas
  • , Klaus Hartung
  • , Dieter Langosch
  • , Hubert Rehm
  • , Ernst Bamberg
  • , Werner W. Franke
  • , Heinrich Betz

Research output: Contribution to journalArticlepeer-review

322 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1050-1053
Number of pages4
JournalScience
Volume242
Issue number4881
DOIs
StatePublished - 1988
Externally publishedYes

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