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.
Copyright 2001 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / chemistry
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Animals
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Binding Sites
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Blotting, Western
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Brain / metabolism
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Calcium / metabolism
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Calmodulin / chemistry
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Calmodulin-Binding Proteins / chemistry*
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DNA, Complementary / metabolism
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Exocytosis
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Glutathione Transferase / metabolism
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Myosin Type V*
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Nerve Tissue Proteins / chemistry*
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Protein Binding
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Protein Biosynthesis
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Protein Structure, Tertiary
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Qa-SNARE Proteins
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R-SNARE Proteins
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Rats
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Recombinant Fusion Proteins / metabolism
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Recombinant Proteins / chemistry
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SNARE Proteins
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Synaptophysin / chemistry
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Vesicular Transport Proteins*
Substances
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Actins
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Calmodulin
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Calmodulin-Binding Proteins
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DNA, Complementary
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Membrane Proteins
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Nerve Tissue Proteins
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Qa-SNARE Proteins
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R-SNARE Proteins
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Recombinant Fusion Proteins
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Recombinant Proteins
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SNARE Proteins
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Synaptophysin
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Vesicular Transport Proteins
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chicken brain myosin-V p190
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Glutathione Transferase
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Myosin Type V
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Calcium