Molecular mechanism of Ca^<2+> channel protein complexes at presynapse.

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In presynapse, vesicles docking in close vicinity to voltage dependent Ca^<2+> channels (VDCCs) is essential for the control of neurotransmitter release triggered by depolarization-induced Ca^<2+> influx. We have recently reported that VDCC β-subunits physically interact with the presynaptic active zone scaffolding protein RIM1. This interaction cooperates with RIM1-Rab3 interaction to support neurotransmitter exocytosis by anchoring vesicles in the vicinity of VDCCs and by maintaining depolarization-triggered Ca^<2+> influx as a result of marked inhibition of voltage-dependent inactivation of VDCCs. In this research, we demonstrate that other RIM proteins (RIM2-4) also exert prominent suppression on VDCC inactivation via direct binding to β-subunits to enhance neurotransmitter release.