A naukri.com initiative
Bioengineer
2w
207
Image Credit: Bioengineer
Autophagy and Lysosomal Pathways Drive Unconventional Secretion of Parkinson’s Disease Protein
- A study by researchers at Doshisha University in Japan reveals a novel mechanism behind the unconventional secretion of PARK7, a protein linked to Parkinson's disease and cellular oxidative stress responses.
- The study sheds light on how autophagy mechanisms orchestrate a secretion process that diverges from traditional protein trafficking pathways.
- Certain proteins, like PARK7, bypass the canonical secretion pathway and use unconventional methods such as direct translocation across the plasma membrane or exocytosis via intracellular vesicles.
- Autophagy, originally known for its role in cellular degradation and recycling, is now recognized as playing a key role in unconventional protein secretion.
- Under oxidative stress, PARK7 is secreted through a sophisticated autophagy-based pathway involving both macroautophagy and chaperone-mediated autophagy (CMA).
- Oxidative insults trigger increased autophagic flux, leading to the formation of 'secretory autolysosomes' that extrude PARK7 outside the cell.
- This unconventional secretion route involving lysosomal delivery via CMA and a specialized SNARE protein complex challenges traditional views on lysosomal function.
- The study highlights how disrupting autophagosome-lysosome fusion or inhibiting lysosomal degradation can impede PARK7 secretion, emphasizing the importance of functional lysosomal compartments.
- Insights from this research expand understanding of autophagy's secretory capabilities and its impact on disease pathology, with implications for therapeutic interventions in neurodegenerative conditions.
- The discovery of PARK7 secretion regulation through secretory autolysosomes opens up new possibilities for biomarker development and early detection of Parkinson's disease.
Read Full Article
12 Likes
For uninterrupted reading, download the app