Aggresomes are cytoplasmic inclusions formed when the proteasome's capacity to degrade misfolded proteins is exceeded. These structures are characterized by the accumulation of ubiquitinated, misfolded proteins at a pericentriolar region, surrounded by a cage of intermediate filament (IF) protein, particularly vimentin. Aggresomes form in response to an overload of aggregation-prone misfolded proteins, which cannot be degraded by the proteasome. The formation of aggresomes is associated with the redistribution of vimentin to form a cage around the pericentriolar core of aggregated proteins. Microtubules (MTs) are essential for aggresome formation, as their disruption prevents aggresome formation. Aggresomes are not limited to CFTR but can also form from other misfolded proteins, such as presenilin-1 (PS1), indicating a general cellular response to protein aggregation. The ultrastructure of aggresomes includes electron-dense particles composed of misfolded proteins, surrounded by a vimentin-based meshwork. These findings suggest that aggresomes are a cellular mechanism to contain and isolate misfolded proteins, preventing their harmful effects on the cell. The formation of aggresomes is a dynamic process involving the reorganization of the cytoskeleton and the redistribution of cellular components to manage the accumulation of misfolded proteins.Aggresomes are cytoplasmic inclusions formed when the proteasome's capacity to degrade misfolded proteins is exceeded. These structures are characterized by the accumulation of ubiquitinated, misfolded proteins at a pericentriolar region, surrounded by a cage of intermediate filament (IF) protein, particularly vimentin. Aggresomes form in response to an overload of aggregation-prone misfolded proteins, which cannot be degraded by the proteasome. The formation of aggresomes is associated with the redistribution of vimentin to form a cage around the pericentriolar core of aggregated proteins. Microtubules (MTs) are essential for aggresome formation, as their disruption prevents aggresome formation. Aggresomes are not limited to CFTR but can also form from other misfolded proteins, such as presenilin-1 (PS1), indicating a general cellular response to protein aggregation. The ultrastructure of aggresomes includes electron-dense particles composed of misfolded proteins, surrounded by a vimentin-based meshwork. These findings suggest that aggresomes are a cellular mechanism to contain and isolate misfolded proteins, preventing their harmful effects on the cell. The formation of aggresomes is a dynamic process involving the reorganization of the cytoskeleton and the redistribution of cellular components to manage the accumulation of misfolded proteins.