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Abstract
p62 bodies form in response to proteotoxic stress and may act as platforms for autophagy-dependent degradation.
- Cells activate stress-response mechanisms to maintain balance when under stress.
- Dysregulation of these processes is linked to diseases like cancer, liver disorders, and neurodegenerative diseases.
- p62 plays a key role in regulating protein balance and stress responses through autophagy and signaling pathways.
- Liquid-liquid phase separation of p62 with ubiquitinated proteins leads to the formation of membraneless structures called p62 bodies.
- These p62 bodies sequester specific proteins and may facilitate both degradation and stress signaling.
- Recent findings suggest a shift in understanding p62 from a simple receptor to a complex signaling hub with higher-order assemblies.
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