Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains.

By Dylan T. Murray, Masato Kato, Yi Lin, K. Thurber, I. Hung, S. McKnight, R. Tycko. Cell, 2017

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Protein Phase Separation: A New Phase in Cell Biology (2018, background): “Initial studies from McKnight and coworkers found that these disordered domains can form reversible hydrogels, and this is dependent on labile kinked beta sheets [39, 77].”
Pi-Pi contacts are an overlooked protein feature relevant to phase separation (2018, background): “…the electrostatic effects of charge patterning (Nott et al., 2015; Lin et al., 2016; Das and Pappu, 2013), multivalency of PTM sites and PTM-binding motifs, and transient structural interactions, including strand formation (Murray et al., 2017) and helical interactions (Conicella et al., 2016).”
FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions (2018, background): “The droplet and hydrogel states are stabilized by hydrogen bonding between antiparallel b sheet motifs formed by core residues 39–95 in the low-complexity (LC) domain (Murray et al., 2017) (Figure 1A).”
A molecular grammar governing the driving forces for phase separation of prion-like RNA binding proteins (2018, neutral): “Based on recent structural studies of the PLD (Murray et al., 2017), glutamine residues could also be required for the formation of labile cross-beta sheets, and therefore it seems possible that this mutation prevents hardening by preventing the formation of such higher order structures.”