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Updated: Aug 12, 2026

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
Published on: October 19, 2012
Globular tail of myosin-V is bound to vamp/synaptobrevin
A Ohyama1, Y Komiya, M Igarashi
1Department of Anesthesiology and Reanimatology, Gunma University School of Medicine, Maebashi, Gunma, 371-8511, Japan.
Abstract:
VAMP/synaptobrevin is one of a number of v-SNAREs involved in vesicular fusion events in neurons. In a previous report, VAMP was shown to form a complex with synaptophysin and myosin V, a motor protein based on the F-actin, and that myosin V was then released from the complex in a Ca(2+)-dependent manner. Here, we found that VAMP alone is bound to myosin V in a Ca(2+)-independent manner, and determined that the globular tail domain of myosin V is its binding site. The syntaxin-VAMP-myosin V formed in the presence of Ca(2+)/calmodulin (CaM). In the absence of CaM, only syntaxin-VAMP, or VAMP-myosin V complex was formed. Our results suggest that VAMP acts as a myosin V receptor on the vesicles and regulates formation of the complex.
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