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Department of Anatomy and Cell Biology, East Carolina University School of Medicine, Greenville, North Carolina 27858
Brain myosin V is a member of a widely distributed class of unconventional myosins that may be of
central importance to organelle trafficking in all eukaryotic cells. Molecular constituents that target this
molecular motor to organelles have not been previously identified. Using a combination of immunopurification, extraction, cross-linking, and coprecipitation assays, we demonstrate that the tail domain of brain
myosin V forms a stable complex with the synaptic vesicle membrane proteins, synaptobrevin II and synaptophysin. While myosin V was principally bound to synaptic vesicles during rest, this putative transport
complex was promptly disassembled upon the depolarization-induced entry of Ca2+ into intact nerve endings.
Coimmunoprecipitation assays further indicate that
Ca2+ disrupts the in vitro binding of synaptobrevin II to
synaptophysin in the presence but not in the absence of
Mg2+. We conclude that hydrophilic forces reversibly
couple the myosin V tail to a biochemically defined
class of organelles in brain nerve terminals.
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