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Regulation of synaptic vesicle fusion by protein kinase C

Sabine Hilfiker and George J. Augustine

Activation of protein kinase C (PKC) by phorbol esters stimulates secretion of neurotransmitters from most presynaptic terminals. This action of PKC may be even more general, because secretion from many non-neuronal cells is also stimulated by these agents. Despite recent advances in our understanding of the molecular mechanisms underlying transmitter release, the mode of action of PKC in nerve terminals remains unclear. PKC activation might enhance the presynaptic Ca²⁺ signal that triggers release, for example by modulating ion channels to increase Ca²⁺ influx or by decreasing Ca²⁺ buffering or removal. Alternatively, PKC could act independently of Ca²⁺ entry, by increasing the number of release sites or releasable vesicles, or by making individual vesicles more sensitive to entering Ca²⁺. Distinguishing among these possible mechanisms has proven difficult, in part because the electrophysiological measurements typically used for such studies provide only indirect information about Ca²⁺ signalling and vesicle trafficking.

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