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J. Biol. Chem., Vol. 269, Issue 40, 24534-24537, 10, 1994
N Calakos and RH Scheller
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.
Vesicle-associated membrane protein and synaptophysin are associated on the synaptic vesicle
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University Medical Center, California 94305.
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