Liquid-liquid phase separation has emerged as a mechanism for cells to organize reactions or sequester mRNA. These membrane-less organelles are primarily made up of RNA and ribonucleoproteins. hnRNPA2, a heterogeneous nuclear ribonucleoprotein, was found to aggregate in multisystem proteinopathy, a rare disease characterized by protein inclusions in diverse tissues. We have shown that hnRNPA2 undergoes liquid-liquid phase separation in vitro. The low complexity domain undergoes phase separation in high salt, while the full-length phase separates in low salt conditions. Using NMR, we showed that the monomeric low complexity domain of hnRNPA2 has a disordered structure. The disease mutation does not greatly affect the disordered structure or intermolecular contacts in the monomer.

Liquid-liquid phase separation of the low complexity domain of hnRNPA2

252nd National Meeting (2016)

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