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Krainer, Georg; Welsh, Timothy J; Joseph, Jerelle A; Espinosa, Jorge R; Wittmann, Sina; de Csilléry, Ella; Sridhar, Akshay; Toprakcioglu, Zenon; Gudiškytė, Giedre; Czekalska, Magdalena A; Arter, William E; Guillén-Boixet, Jordina; Franzmann, Titus M; Qamar, Seema; George-Hyslop, Peter St; Hyman, Anthony A; Collepardo-Guevara, Rosana; Alberti, Simon; Knowles, Tuomas P J
Nature communications, 02/2021, Letnik: 12, Številka: 1Journal Article
Liquid-liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological function and malfunction. Here we show that cellular proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, can reenter a phase-separated regime at high salt concentrations. By bringing together experiments and simulations, we demonstrate that this reentrant phase transition in the high-salt regime is driven by hydrophobic and non-ionic interactions, and is mechanistically distinct from the low-salt regime, where condensates are additionally stabilized by electrostatic forces. Our work thus sheds light on the cooperation of hydrophobic and non-ionic interactions as general driving forces in the condensation process, with important implications for aberrant function, druggability, and material properties of biomolecular condensates.
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