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Complexin-3 is a cytosolic neuronal protein that regulates the SNARE complex-mediated synaptic vesicle fusion, a critical step in neurotransmitter release at synapses[1][5][6]. Complexin-3 is predominantly found in the retina, where it is essential for the maintenance of synaptic ultrastructure and efficient neurotransmission, especially at photoreceptor ribbon synapses[1][3][7]. It acts as both a clamp that suppresses spontaneous vesicle fusion in the absence of calcium influx and a facilitator that enhances transmitter release upon stimulation[3][6]. Mutations or deletions affecting Complexin-3 can result in aberrant synaptic function and neurodevelopmental disorders. Complexin-3 is a member of a small family (including Complexins 1-4), specifically binding to SNARE complexes but not directly to other receptor, channel, or transporter structures[4][5][6]. Currently, it is not considered a direct therapeutic target, and there are no approved drugs or clinical biomarkers associated with this protein.
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