The accumulation of protein aggregates poses a significant burden on cellular fitness and is linked to several neurodegenerative pathologies. Aggrephagy represents a key defense mechanism of our cells against protein aggregation. During this process, cells grow a double-layered membrane structure, called the autophagosome, which encloses the cargo and delivers it to the lysosome for degradation. The initiation of aggrephagy depends on cargo recognition by autophagy receptor proteins. In Alzheimer’s disease (AD), the protein Tau co-aggregates with the autophagy receptor p62. Despite recognition by p62, Tau aggregates evade autophagic degradation and accumulate in the brains of AD patients, which correlates with disease progression. To address why autophagic degradation of Tau aggregates is impaired and whether autophagy can in principle degrade such fibrillar cargo, we employ a combination of cell biological methods, chemical-induced tethering, and biochemical assays. Our work aims to shed light on the mechanistic barriers to the autophagic degradation of pathogenic protein aggregates.