An Atypical Unfolded Protein Response in Heat Shocked Cells
Author Information
Author(s): Heldens Lonneke, Hensen Sanne M. M., Onnekink Carla van, Dirks Siebe T., Lubsen Ron P., Cotterill Sue
Primary Institution: Department of Biomolecular Chemistry, Radboud University Nijmegen, Nijmegen, The Netherlands
Hypothesis
How are resources allocated when both the heat shock response and the unfolded protein response are active?
Conclusion
Heat stress activates the initial step of the unfolded protein response, but the subsequent transcriptional activation is blocked, indicating a non-productive response.
Supporting Evidence
- Heat stress induces the synthesis of canonical UPR transcription factors.
- The DNAJB9 promoter is activated by heat stress independently of XBP1s.
- eIF2α phosphorylation is crucial for the activation of UPR promoters during heat stress.
Takeaway
When cells get too hot, they try to fix their proteins, but they can't finish the job properly, which can lead to problems.
Methodology
The study involved heat shocking HEK293 cells and analyzing the activation of UPR and HSR pathways through various assays.
Limitations
The study primarily focuses on HEK293 cells, which may not fully represent other cell types or conditions.
Digital Object Identifier (DOI)
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