Autophagy is a lysosomal-dependant pathway mediating the degradation of aggregated proteins (aggrephagy) and dysfunctional mitochondria (mitophagy). Autophagy is the only method that releases iron from the intracellular storage protein ferritin (ferritinophagy). As iron accumulation accompanies aggregated α-synuclein in disease (synucleinopathies), we aimed to assess if iron overload is consequent to diminished autophagic flux. To investigate ferritinophagy impairment, we used human post-mortem brain tissue from 6 patients with pathologically confirmed Lewy body dementia (DLB) and multiple system atrophy (MSA), assessing the hippocampus, frontal, and temporal lobe. Using a spinning disk confocal microscope, we assessed autophagy function by immunostaining for ferritin and autophagy markers (i.e., LC3B). Images were acquired as Z-stacks and assessed within a 3D context. Indeed, we confirmed that ferritin accumulates within glial cells of synucleinopathies, most significantly within MSA. We uniquely found significant intraneuronal ferritin accumulation within DLB tissue compared to healthy controls. We further identified that ferritin in DLB tissue colocalises with LC3B, supporting that observed ferritin is accumulating within autophagosomes and cannot be cleared. Moreover, ferritin significantly colocalised with α-synuclein, possibly indicating that protein aggregates directly hinder the autophagosome-lysosome fusion, a phenotype we have also observed in cell culture models of α-synuclein aggregation. Thus, we have illustrated that autophagy impairment is a true consequence of α-synuclein aggregation, particularly within patient pathologies. Therapies targeting the restoration of autophagy will likely provide significant neuroprotective benefits in clinical settings.