A highly Ca(2+)-sensitive pool of vesicles is regulated by protein kinase C in adrenal chromaffin cells

We have used flash photolysis of caged Ca(2+) and membrane capacitance measurements to probe exocytosis in chromaffin cells at low concentrations of intracellular Ca(2+) ([Ca(2+)](i)) (<10 μM). We observed a small pool of granules that is more sensitive to [Ca(2+)](i) than the previously described “readily releasable pool.” Upon activation of PKC, this “highly Ca(2+)-sensitive pool” is enhanced in size to a greater extent than the readily releasable pool but is eliminated upon expression of a C-terminal deletion mutant (Δ9) of synaptosome-associated protein of 25 kDa (SNAP-25). Thus, in chromaffin cells, PKC enhances exocytosis both by increasing the number of readily releasable vesicles and by shifting vesicles to a highly Ca(2+)-sensitive state, enabling exocytosis at sites relatively distant from Ca(2+) channels.