Cardiac L-type Ca channels are multi-protein complexes including accessory subunits such as Ca_V2 that increase current. Members of the RGK family of small GTPases decrease current, although the mechanism remains poorly defined. In this study we evaluated the contribution of the L-type Ca channel -subunit (Ca_V1.2) to Ca_V2-Rem inhibition of Ca channel current. Specifically, we addressed whether protein kinase A (PKA) modulation of Ca_V1.2 modifies Ca_V2-Rem inhibition of Ca channel current. We first tested the effect of Rem on Ca_V1.2 in HEK 293 cells. Rem co-expression with Ca_V1.2reduces Ba current expression under basal conditions, and Ca_V2a co-expression enhances Rem block of Ca_V1.2 current. Surprisingly, PKA inhibition by 133 nM H-89, or 50 µM Rp-cAMPS partially relieved the Rem-mediated inhibition of current activity both with and without Ca_V2a. Also, current through the PKA-insensitive Ca_V1.2 mutant, serine1928alanine (Ca_V1.2-S1928A), was not inhibited by Rem, and co-expression with Ca_V|*beta*|2a was not completely blocked by Rem, suggesting that the phosphorylation of S1928 contributes to Rem-mediated Ca channel modulation. As a model for native Ca channel complexes we tested the ability of Rem over-expression in HIT-T15 cells and embryonic ventricular myocytes to interfere with native current. Native current is also sensitive to Rem block, and H-89 pretreatment relieves the ability of Rem to regulate Ca current. We conclude that Rem is capable of regulating L-type current, that release of Rem block is modulated by cellular kinase pathways, and that Ca_V1.2-C-terminus contributes to Rem-dependent channel inhibition.