CAPRIN1 condensates shift immature SOD1 toward unfolding and aggregation
Original source
Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates. (opens in a new tab)Compass summarised this from the study's abstract.
Study details
- Studied in
- Human
Related topics
A nuclear magnetic resonance study found that CAPRIN1, a stress-granule protein, preferentially interacts with unfolded immature superoxide dismutase 1 (SOD1), shifting it toward an unfolded state. Unfolding in CAPRIN1 condensates was linked to aggregation, while zinc-bound dimeric SOD1 was less susceptible to unfolding.
Why this matters
The findings provide a molecular explanation for how stress-granule environments could influence SOD1 misfolding and aggregation, which is relevant to ALS research. This is a laboratory, mechanistic finding and does not currently change treatment for people with ALS.
Limitations and context
The study used solution nuclear magnetic resonance and condensate models rather than people or clinical samples. It examined specific biochemical forms of SOD1 and CAPRIN1, so the relevance to ALS in patients remains to be established. The work supports a hypothesis about ALS mutations affecting metal binding or dimerization but does not test treatments or patient outcomes.