Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle.
The synaptic vesicle membrane protein VAMP (vesicle-associated membrane protein or synaptobrevin) has been implicated in synaptic vesicle docking and fusion. Synaptophsin (p38), also a synaptic vesicle membrane protein, has four transmembrane domains and may function as a gap junction-like pore or channel. Here we report evidence for a direct interaction between VAMP and synaptophysin using chemical cross-linking followed by the identification of immunoreactive protein complexes. A prominent complex of 56 kDa was found to consist of VAMP and synaptophysin. Furthermore, we demonstrate that this VAMP-synaptophysin complex is enriched in the synaptic vesicle fraction of rat brain, is independent of detergent solubilization, and is present in PC12 cells subjected to in vivo cross-linking.
Calakos
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N
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical Center, California 94305.
Scheller
R H
RH
D000818:Animals; D008565:Membrane Proteins / Q000032:analysis*; D009419:Nerve Tissue Proteins / Q000032:analysis*; D050683:R-SNARE Proteins; D051381:Rats; D017207:Rats, Sprague-Dawley; D013572:Synaptic Vesicles / Q000737:chemistry*; D016708:Synaptophysin / Q000032:analysis*
D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050683:R-SNARE Proteins; D016708:Synaptophysin