bioRxivBiochemistry
Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domains
L. Guo, J. R. Mann, J. C. Mauna, K. E. Copley, H. Wang, J. D. Rubien, H. M. Odeh, J. Lin, B. L. Lee, L. Ganser, E. Robinson, K. M. Kim, A. C. Murthy, T. Paul, B. Portz, A. M. Gleixner, Z. Diaz, J. L. Carey, A. Smirnov, G. Padilla, E. Lavorando, C. Espy, Y. Shang, E. J. Huang, A. Chesi, , J. Shorter
Abstract
RNA-binding proteins with prion-like domains, such as FUS and TDP-43, condense into functional liquids, which can transform into pathological fibrils that underpin fatal neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS)/frontotemporal dementia (FTD). Here, we define short RNAs (24-48 nucleotides) that prevent FUS fibrillization by promoting liquid phases, and distinct short RNAs that prevent and, remarkably, reverse FUS condensation and fibrillization. These activities require interactions with multiple RNA-binding domains of FUS and are encoded by RNA sequence, length, and structure. Importantly, we define a short RNA that dissolves aberrant cytoplasmic FUS condensates, restores nuclear FUS, and mitigates FUS proteotoxicity in optogenetic models and human motor neurons. Another short RNA dissolves aberrant cytoplasmic TDP-43 condensates, restores nuclear TDP-43, and mitigates TDP-43 proteotoxicity. Since short RNAs can be effectively delivered to the human brain, these oligonucleotides could have therapeutic utility for ALS/FTD and related disorders.
- organism: human
- assay: bulk RNA-seq
- research focus: drug response / drug discovery
- research focus: cell signaling & trafficking
- research focus: protein folding & dynamics
- approach: experimental assay
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