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Extracellular Vesicle‐Mediated Delivery of 20S Proteasomes Enhances Tau Degradation in Recipient Cells
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Extracellular Vesicle‐Mediated Delivery of 20S Proteasomes Enhances Tau Degradation in Recipient Cells
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Journal Article
Extracellular Vesicle‐Mediated Delivery of 20S Proteasomes Enhances Tau Degradation in Recipient Cells
2025
Overview
The 26S proteasome holoenzyme comprises 20S catalytic and 19S regulatory complexes. Accumulating evidence suggests that the majority of proteasomes in the extracellular space exist as free 20S proteasomes; however, their origin and pathophysiological function remain to be determined. Here, we report that cellular proteasomes are effectively packaged into the lumen of extracellular vesicles (EVs) and secreted in a structurally intact and enzymatically active 20S form. We further demonstrate that EV‐encapsulated 20S proteasomes are delivered to recipient cells and facilitate the degradation of overexpressed tau proteins without disrupting global proteolytic pathways. These findings highlight a novel cell‐to‐cell communication system that transports the proteasomes to target cells for the clearance of proteotoxic substrates. Further characterisation of this homeostatic mechanism will improve our understanding of organismal stress response mechanisms and may provide a therapeutic approach to treat various proteinopathies, including Alzheimer's disease. This study demonstrates that the 20S proteasomes are packaged into extracellular vesicles (EVs), secreted as an active proteolytic enzyme and transferred to recipient cells. These EV‐encapsulated proteasomes selectively degrade excess proteins, highlighting a novel mechanism of a cell‐to‐cell communication system that supports proteostasis and proteome remodelling.
Publisher
John Wiley & Sons, Inc,John Wiley and Sons Inc,Wiley
