Electrical activity in neurons is shaped by the activity of multiple classes of voltage-gated Ca2+ channels (VGCCs). These channels permit the flux of Ca2+ into cells following membrane depolarizations, and these channels drive essential cellular functions in the brain, including activity-dependent gene transcription, neuronal growth and development, pace-making activity, and neurotransmission. The activity of VGCCs is tightly regulated, and disruption of the normal function of these channels can result in multiple forms of disease, including life-altering neurological syndromes. One key regulator of VGCC activity is the Ca2+ sensor, calmodulin (CaM). CaM confers a remarkable ability to VGCCs to modulate their activity in response to changes in cellular Ca2+ concentration. This form of regulation permits these channels to precisely tune their activity in response to a varied array of cellular requirements in different physiological contexts. Mutations in CaM that lead to deficits in CaM-dependent regulation of VGCCs have been identified as contributing to diseases termed calmodulinopathies, which are frequently characterized by cardiac and neurological impairments. Though prior research has revealed a number of important mechanisms by which these mutations participate in cardiac dysfunction via VGCC dysregulation, the relationship between CaM mutations and neurological symptoms observed in patients is less well understood. In this work, I demonstrate that mutant CaM variants identified in patients with cardiac and neurological symptoms are able to confer dysregulated channel behavior on VGCCs that are essential to healthy neurological function. Using a heterologous expression system, I explore the biophysical properties of these neuronal channels in the context of selected CaM mutants and show that typical Ca2+-dependent regulation via CaM is frequently disrupted by these mutants. This work focuses primarily on a region of CaM that harbors mutations that are particularly impactful on these channel properties, indicating a similar mechanism to that which is known to cause disrupted CaM-dependent regulation of cardiac VGCCs. Additionally, protein binding assays show that many of these pathological CaM mutants readily associate with the CaM-binding elements of the VGCCs found in neurons, implying a physiological relevance for the disrupted regulation these mutations impose. In summary, this work gives a background to help contextualize the importance of VGCC regulation in neurological health and provides evidence that CaM mutants identified in patients exhibiting multiple distinct neurological symptoms including schizophrenia, developmental delay, and autism spectrum disorder, may act through disrupted VGCC regulation to participate in neurological disease.