Hsp40 and CSPα Chaperone Complex in Heat Shock Response
Author Information
Author(s): Gibbs Sarah J., Barren Brandy, Beck Katy E., Proft Juliane, Zhao Xiaoxi, Noskova Tatiana, Braun Andrew P., Artemyev Nikolai O., Braun Janice E. A.
Primary Institution: University of Calgary
Hypothesis
How do stress-induced chaperones protect synaptic transmission and prevent neurodegeneration?
Conclusion
Hsp40 associates with the CSPα chaperone complex during heat shock, enhancing neuroprotection.
Supporting Evidence
- Hsp40 becomes a major component of the CSPα complex after heat shock.
- Association of Hsp40 with CSPα enhances GTP hydrolysis of Gαs.
- Transient assembly of Hsp40 with CSPα is important for synaptic function.
- Heat shock response modulates signaling through Gαs pathways.
Takeaway
When cells get stressed, a helper protein called Hsp40 teams up with another protein, CSPα, to protect brain cells from damage.
Methodology
The study involved evaluating the interaction between Hsp40 and CSPα in response to heat shock and pharmacological treatments using various cell lines.
Limitations
The study primarily used in vitro models, which may not fully replicate in vivo conditions.
Statistical Information
P-Value
0.0023
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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