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A PKA consensus phosphorylation site S1928 at the   α    1 1.2 subunit of the rabbit cardiac L-type channel, Ca V 1.2, is involved in the regulation of Ca V 1.2 kinetics and affects catecholamine secretion. This mutation does not alter basal Ca V 1.2 current properties or regulation of Ca V 1.2 current by PKA and the beta-adrenergic receptor, but abolishes Ca V 1.2 phosphorylation by PKA. Here, we test the contribution of the corresponding PKA phosphorylation site of the human   α    1 1.2 subunit S1898, to the regulation of catecholamine secretion in bovine chromaffin cells. Chromaffin cells were infected with a Semliki-Forest viral vector containing either the human wt or a mutated S1898A   α    1 1.2 subunit. Both subunits harbor a T1036Y mutation conferring nifedipine insensitivity. Secretion evoked by depolarization in the presence of nifedipine was monitored by amperometry. Depolarization-triggered secretion in cells infected with either the wt   α    1 1.2 or   α    1 1.2/S1898A mutated subunit was elevated to a similar extent by forskolin. Forskolin, known to directly activate adenylyl-cyclase, increased the rate of secretion in a manner that is largely independent of the presence of S1898. Our results are consistent with the involvement of additional PKA regulatory site(s) at the C-tail of   α    1 1.2, the pore forming subunit of Ca V 1.2.

The Involvement of Ser1898 of the Human L-Type Calcium Channel in Evoked Secretion