Exploring how Hsp70 phosphorylation affects protein folding and cell stress responses
Official title: Understanding the role of Hsp70 phosphorylation in proteostasis
Funded at University of North Carolina Charlotte · NIH-11136347 · Data updated 2026-11-12
This study looks at how a special protein called Hsp70 helps cells stay healthy and function well when they're under stress, like heat, by checking how certain changes to Hsp70 affect its job in keeping other proteins in shape; it's mainly done in yeast but could help us understand how our own cells handle stress better.
Quick facts
| Grant type | R01 grant |
|---|---|
| Study type | NIH-funded research |
| Funding institution | University of North Carolina Charlotte NIH-funded |
| Lab location | 1 site (Charlotte, United States) |
| Project start | July 10, 2024 |
| Project end | May 31, 2028 |
| Funding year | 2025 |
| Award (this year) | $319,730 |
| NIH project number | 5R01GM149639-02 |
| Project ID | NIH-11136347 on NIH RePORTER |
Who could benefit from this research
✓Could help
Ideal candidates for this research are individuals with degenerative neurological conditions or those affected by cellular stress-related diseases.
✕Less likely to help
Patients with conditions unrelated to cellular stress responses or protein misfolding may not benefit from this research.
What this research studies
This research investigates the role of Hsp70, a crucial molecular chaperone, in maintaining protein stability and function under stress conditions. The study focuses on how specific phosphorylation sites on Hsp70 influence its ability to manage protein folding and cellular responses to heat stress. By examining these mechanisms in yeast, the research aims to uncover the relationship between Hsp70 phosphorylation and the formation of stress granules and protein aggregates. This could provide insights into how cells cope with stress and maintain their integrity.
Why it matters
Potential benefit: If successful, this research could lead to new strategies for treating degenerative diseases by enhancing cellular stress responses.
How similar studies have gone: Previous research has shown that understanding molecular chaperones like Hsp70 can lead to significant advancements in treating related diseases, indicating a promising avenue for this investigation.
Where this research is happening
-
University of North Carolina Charlotte
Charlotte, United States Active
Researchers
- Principal investigator: Truman, Andrew William — University of North Carolina Charlotte
- Study coordinator: Truman, Andrew William
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About this research
- This is an active NIH-funded research project — typically early-stage science, not a clinical trial accepting patient enrollment.
- Some NIH-funded labs run parallel clinical studies or seek volunteers for related work. To check, contact the principal investigator or institution listed above.
- For full project details, budget, and progress reports, visit the official NIH RePORTER page.