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Exploring the Structural Order of Condensates Formed by the PRD2 Domain of Mouse CPEB3
Faina Pinhero1, Dhanya S Reselammal1, Arunima Sandeep1
1School of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram, Maruthamala PO, Vithura, Trivandrum, Kerala 695551, India.
ACS Chemical Neuroscience
|August 5, 2025
Summary
The mouse prion-like protein mPRD2 forms stable, solid amyloid condensates via phase separation. This unique self-assembly mechanism is crucial for long-term memory and synaptic connections.
Area of Science:
- Neuroscience
- Biochemistry
- Structural Biology
Background:
- Long-term memory relies on stable synaptic connections.
- The prion-like protein CPEB3 (cytoplasmic polyadenylation element binding protein isoform 3) mediates these connections through its prion-like transformation.
- The N-terminal prion domain, comprising PRD1 and PRD2, is key to CPEB3's prion-like properties.
Purpose of the Study:
- To investigate the in vitro aggregation properties and structural characteristics of mouse PRD2 (mPRD2).
- To understand the role of mPRD2 in forming cellular condensates relevant to memory formation.
Main Methods:
- In vitro phase separation assays.
- Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy.
- Biophysical characterization techniques.
Main Results:
- Mouse PRD2 undergoes phase separation at low concentrations.
- mPRD2 forms stable, solid, amyloid-like condensates, deviating from typical liquid phase separation.
- Solid-state NMR and biophysical studies identified mixed secondary structures within the mPRD2 condensates.
Conclusions:
- The unique phase separation behavior of mPRD2, leading to rigid, amyloid-like self-assembly, is attributed to its amino acid sequence and conformational changes.
- This self-assembly mechanism contributes to the stable synaptic connections essential for long-term memory.
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