Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
2006
How Cells Manage Unfolded Proteins
publication
Evidence: high
Author Information
Author(s): Sebastián Bernales, Kent L. McDonald, Peter Walter
Primary Institution: Howard Hughes Medical Institute, University of California San Francisco
Hypothesis
Does autophagy help cells cope with the stress of unfolded proteins in the endoplasmic reticulum?
Conclusion
The study found that autophagy is crucial for cell survival during endoplasmic reticulum stress by sequestering unfolded proteins.
Supporting Evidence
- Yeast cells expand their endoplasmic reticulum volume significantly under stress.
- Autophagosome-like structures form in response to unfolded proteins.
- Cell survival during ER stress does not require vacuolar proteases.
Takeaway
When cells have too many unfolded proteins, they can use a process called autophagy to help manage and remove them, keeping the cell healthy.
Methodology
The study used electron microscopy to observe changes in yeast cells under stress conditions and analyzed the formation of autophagosome-like structures.
Digital Object Identifier (DOI)
Want to read the original?
Access the complete publication on the publisher's website