Abstract
The effect of latrunculin A, an inhibitor of actin cross-linking, on exocytosis in PC12 cells was investigated with single cell amperometry. This analysis strongly suggests that the actin cytoskeleton might be involved in regulating exocytosis, especially by mediating the constriction of the pore. In an extended kiss-and-run release mode, actin could actually control the fraction of neurotransmitters released by the vesicle. This scaffold appears to contribute, with the lipid membrane and the protein machinery, to the closing dynamics of the pore, in competition with other forces mediating the opening of the exocytotic channel.