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RNA G-Quadruplexes Function as a Tunable Switch of FUS Phase Separation.

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RNA G-quadruplexes (rG4s) can control the phase separation of FUS proteins. Specific rG4 structures inhibit toxic FUS aggregation, offering a new therapeutic strategy for neurodegenerative diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • FUS protein undergoes liquid-liquid phase separation (LLPS) for cellular functions.
  • Aberrant FUS phase transitions are linked to neurodegenerative diseases.
  • RNA oligonucleotides can reverse toxic FUS aggregation, but their mechanisms are unclear.

Purpose of the Study:

  • To identify structural determinants of RNA that modulate FUS LLPS.
  • To investigate RNA G-quadruplexes (rG4s) as regulators of FUS phase behavior.
  • To develop RNA-based therapeutics for FUS-related disorders.

Main Methods:

  • Investigated the effect of rG4 structure, concentration, length, and stability on FUS LLPS.
  • Utilized a bioinformatic pipeline to discover novel rG4 inhibitors.
  • Analyzed FUS-RNA interactions using biophysical techniques.

Main Results:

  • Identified rG4s as potent modulators of FUS LLPS.
  • Demonstrated that rG4 activity is tunable by length and stability, switching between inhibition and nucleation.
  • Showed that stabilized rG4s inhibit FUS assembly and resist ionic disruption.
  • Discovered that short rG4s preferentially interact with soluble FUS, promoting dispersion.
  • Uncovered new rG4 inhibitors that reverse FUS LLPS and aggregation.

Conclusions:

  • rG4s are chemically programmable regulators of protein phase behavior.
  • RNA secondary structure dictates functional outcomes in protein condensates.
  • rG4s offer a blueprint for RNA-based therapeutics targeting pathogenic FUS assemblies.
  • Established a structure-function paradigm for RNA control of biomolecular condensates.