Nucleic Acids ResearchBiochemistryPeer-reviewed journal article
RNA G-Quadruplexes Function as a Tunable Switch of FUS Phase Separation
Jenny L. CareyiD, Miyuki HayashiiD, Emily M. Welebob, Laura R. GanseriD, Huan WangiD, Kerry BuckhaultsiD, Jacquelyn A. DePierro, Zheng ShiiD, James ShorteriD, Sua MyongiD, Aaron R. HaeusleriD, Lin E. GuoiD
Abstract
FUS undergoes liquid-liquid phase separation (LLPS) to support essential cellular functions, but aberrant phase transitions promote toxic aggregation in neurodegenerative disease. Short RNA oligonucleotides can reverse this behavior, yet the structural determinants that govern RNA activity remain poorly defined. Here, we identify RNA G-quadruplexes (rG4s) as tunable structural motifs that potently modulate FUS LLPS. rG4 activity depends on its concentration and is modulated by rG4 length and stability: increasing repeat number switches rG4s from inhibitor to nucleator of FUS assembly, whereas chemical modifications that stabilize rG4 enhance inhibitory function and render these activities resilient to ionic perturbation. Although short rG4s interact with both soluble and condensed FUS, they preferentially engage the soluble pool, likely shifting the equilibrium toward dispersion. Leveraging these mechanistic insights, we developed a bioinformatic pipeline that uncovered more rG4 inhibitors that robustly reverse FUS LLPS and aggregation. Our findings establish rG4s as chemically programmable regulators of protein phase behavior and provide a blueprint for engineering RNA-based therapeutics that dissolve pathogenic FUS assemblies. More broadly, this work directly links RNA secondary structure to distinct functional outcomes in phase behavior, establishing a structure-function paradigm for RNA control of condensates, demonstrating implications in both fundamental biology and therapeutic development. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=81 SRC="FIGDIR/small/685846v1_ufig1.gif" ALT="Figure 1"> View larger version (21K): org.highwire.dtl.DTLVardef@1db3ea8org.highwire.dtl.DTLVardef@eec825org.highwire.dtl.DTLVardef@96187eorg.highwire.dtl.DTLVardef@2204ce_HPS_FORMAT_FIGEXP M_FIG C_FIG
- Citations
- 5
- FWCI
- 8.19
- Field percentile
- top 3%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Visualizing TERRA RNA G-quadruplex unfolding in FUS biomolecular condensates
Tongyin Zheng, Nicolas Lux Fawzi·Journal of Molecular BiologyPeer-reviewed·Mar 6, 2026
- RNA modulates FUS condensate assembly, dynamics, and aggregation through diverse molecular contacts
Tongyin Zheng, Kandarp A. Sojitra, … Nicolas Lux Fawzi·bioRxiv·Dec 13, 2025
- The Structured RNA-binding Domains and Condensation Capacity of FUS Shape its RNA-binding Landscape and Function.
Daniel Jutzi, Juan Alcalde, … Marc‐David Ruepp·bioRxiv·Feb 22, 2026
- Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domains
L. Guo, J. R. Mann, … J. Shorter·bioRxiv·Sep 4, 2023
- Massively parallel characterization of RNA G-quadruplex stability and molecular recognition
Justin G. Martyr, Bryan B. Guzmán, … Daniel Dominguez·Nucleic Acids ResearchPeer-reviewed·Aug 7, 2026
- Small molecule chaperones facilitate the folding of long-non coding RNA
P. Lejault, L. Prudent, … J.-P. Perreault·bioRxiv·Apr 4, 2023