Caveolins are membrane scaffolding proteins that associate with and regulate a variety of signalling proteins, including ion channels. A deficiency in caveolin‐3 (Cav‐3), the major striated muscle isoform, is responsible for skeletal muscle disorders, such as limb‐girdle muscular dystrophy 1C (LGMD 1C). The molecular mechanisms leading to the muscle wasting that characterizes this pathology are poorly understood. Here we show that a loss of Cav‐3 induced by the expression of the LGMD 1C‐associated mutant P104L (Cav‐3P104L) provokes a reduction by half of the maximal conductance of the voltage‐dependent L‐type Ca2+ channel in mouse primary cultured myotubes and fetal skeletal muscle fibres. Confocal immunomiscrocopy indicated a colocalization of Cav‐3 and Cav1.1, the pore‐forming subunit of the L‐type Ca2+ channel, at the surface membrane and in the developing T‐tubule network in control myotubes and fetal fibres. In myotubes expressing Cav‐3P104L, the loss of Cav‐3 was accompanied by a 66% reduction in Cav1.1 mean labelling intensity. Our results suggest that Cav‐3 is involved in L‐type Ca2+ channel membrane function and localization in skeletal muscle cells and that an alteration of L‐type Ca2+ channels could be involved in the physiopathological mechanisms of caveolinopathies.