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Endoplasmic reticulum stress triggers autophagy.
Tomohiro Yorimitsu1, Usha Nair, Zhifen Yang
1Life Sciences Institute, University of Michigan, Ann Arbor, Michigan 48109, USA.
The Journal of Biological Chemistry
|August 12, 2006
Summary
Endoplasmic reticulum (ER) stress, caused by misfolded proteins, triggers autophagy, a cellular recycling process. This study reveals ER stress activates autophagy through the Atg1 kinase pathway, independent of nutrient limitation.
Area of Science:
- Cell Biology
- Molecular Biology
- Stress Response
Background:
- Eukaryotic cells possess stress response mechanisms, including autophagy, crucial for nutrient limitation.
- Autophagy degrades and recycles cellular components like proteins and organelles.
Purpose of the Study:
- To investigate a novel pathway for autophagy induction.
- To determine if endoplasmic reticulum (ER) stress can induce autophagy.
Main Methods:
- Studied the effects of misfolded protein accumulation in the ER on autophagy.
- Analyzed the role of Atg proteins and Atg1 kinase activity in ER stress-induced autophagy.
Main Results:
- ER stress activates the unfolded protein response and stimulates pre-autophagosomal structure assembly.
- Autophagosome formation and transport to the vacuole are dependent on Atg proteins.
- Atg1 kinase activity is elevated during ER stress-induced autophagy, similar to starvation-induced autophagy.
Conclusions:
- Endoplasmic reticulum stress is a novel inducer of autophagy.
- The Atg1 kinase pathway is involved in mediating autophagy in response to ER stress.