Voltage sensitive calcium channels (VSCCs) mediate Ca²⁺ permeability in osteoblasts. Association between VSCC ₁ and subunits targets channel complexes to the plasma membrane and modulates function. In mechanosensitive tissues, a 700kDa ahnak protein anchors VSCCs to the actin cytoskeleton, via the ₂ subunit of the L-type Ca_v1.2 (_1C) VSCC complex. Ca_v1.2 is the major ₁ subunit in osteoblasts, but the cytoskeletal complex and subunit composition are unknown. Among the four subtypes, ₂ and to a lesser extent ₃ subunits, co-immunoprecipitated with the Ca_v1.2 subunit in MC3T3-E1 preosteoblasts. Fluorescence resonance energy transfer (FRET) revealed a complex between Ca_v1.2 and ₂ subunits and demonstrated their association in the plasma membrane and secretory pathway. Western blot and immunohistochemistry showed ahnak association with the channel complex in the plasma membrane via the ₂ subunit. Cytochalasin D exposure disrupted the actin cytoskeleton, but did not disassemble or disrupt the function of the complex of L-type VSCCs Ca_v1.2, ₂ subunit and ahnak. Likewise, siRNA knockdown of ahnak did not disrupt the actin cytoskeleton, but significantly impaired Ca²⁺ influx. Collectively, we showed that Ca_v1.2, ₂ subunit and ahnak form a stable complex in osteoblastic cells which permits Ca²⁺ signaling independently of association with the actin cytoskeleton.