Syntaphilin was initially identified in a yeast two-hybrid screen with the carboxy terminal region of Syntaxin-1 as bait. Syntaxin-1 is a key component of the synaptic vesicle docking machinery that forms the SNARE complex with synaptobrevin and SNAP-25. Syntaphilin competes with SNAP-25 for binding to syntaxin-1 and inhibits the formation of the SNARE complex, thereby potentially regulating synaptic vesicle exocytosis. Syntaphilin also binds dynamin-1 and inhibits dynamin-dependent endocytosis. Mice lacking syntaphilin show an increased level of mitochondrial motility and a reduced density of axonal mitochondria. This correlates with an enhanced short-term facilitation and significant impairments in motor ability, suggesting syntaphilin plays a major role in presynaptic function. Despite its predicted molecular weight, Syntaphilin usually migrates at higher molecular weight in SDS-PAGE. Multiple isoforms are known to exist.

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