Alpha-synuclein (α-synuclein), a key component of Lewy body pathology, is a hallmark of Parkinson's disease. In previous studies, we examined dopaminergic neuron-specific Atg7 autophagy-deficient mice and observed α-synuclein aggregation in vivo. Notably, p62 accumulation preceded synuclein deposition, resulting in the formation of inclusions containing both α-synuclein and p62. This pathological process led to dopamine neuron loss and age-related motor impairments, such as hindlimb defects in 120-week-old mice. In this study, we developed a mouse model by crossing human α-synuclein bacterial artificial chromosome transgenic mice with dopaminergic neuron-specific Atg7 conditional knockout mice to investigate these mechanisms further. The mice exhibited accelerated Lewy body-like pathology and motor dysfunction, providing additional evidence that autophagy deficiency exacerbates synuclein toxicity in vivo. Phosphorylated synuclein deposits were detected in the substantia nigra, hippocampus, and cortical regions reliant on dopaminergic pathways. Degeneration of dopaminergic neurons in the substantia nigra pars compacta was also observed, with neuron numbers declining with age. Interestingly, this mouse model displayed more severe motor deficits than Atg7 autophagy-deficient mice. This novel model offers a valuable platform for studying the interplay between α-synuclein expression, autophagy dysfunction, and neurodegeneration, as well as for testing therapeutic strategies targeting synucleinopathies. Our findings highlight the importance of aging in the manifestation of synuclein toxicity, mirroring the progression observed in patients with Parkinson's disease.