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Synaptotagmin 10 (SYT10) is a member of the synaptotagmin family of integral membrane proteins characterized by a single transmembrane region and two C2 domains that mediate calcium binding and phospholipid interaction[1][3]. Synaptotagmin 10 functions as a calcium sensor specifically required for the calcium-dependent exocytosis of secretory vesicles, including those containing insulin-like growth factor 1 (IGF1), in neurons of the olfactory bulb[1]. It is involved in processes regulating exocytosis and sensory perception of smell, but is not implicated in classical synaptic vesicle exocytosis[1]. Like other calcium-binding synaptotagmins, SYT10 participates in vesicle fusion events and acts via binding to phospholipids and SNARE complexes in a calcium-dependent manner, contributing to regulated membrane fusion in response to increased intracellular calcium[1][2][3]. Mutations or altered function in SYT10 have been linked to rare diseases such as mitochondrial complex I deficiency and arrhythmogenic right ventricular cardiomyopathy[1]. No direct drug interactions are currently known, and it is not generally considered a direct therapeutic target but plays important roles in neuronal secretion mechanisms.
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