@article{31,
  author = {Georg Krainer and Timothy Welsh and Jerelle Joseph and Jorge Espinosa and Sina Wittmann and Ella de Csill{\'e}ry and Akshay Sridhar and Zenon Toprakcioglu and Giedre Gudi{\v s}kyte and Magdalena Czekalska and William Arter and Jordina Guill{\'e}n-Boixet and Titus Franzmann and Seema Qamar and Peter St George-Hyslop and Anthony Hyman and Rosana Collepardo-Guevara and Simon Alberti and Tuomas Knowles},
  title = {Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.},
  abstract = {<p>Liquid-liquid phase separation\&nbsp;of proteins underpins the formation of membraneless compartments in living cells.\&nbsp;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\&nbsp;proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, and Annexin A11,\&nbsp;can reenter a phase-separated regime at high salt concentrations. By bringing together experiments and simulations, we demonstrate that this\&nbsp;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.</p>
},
  year = {2021},
  journal = {Nature communications},
  volume = {12},
  pages = {1085},
  issn = {2041-1723},
  doi = {10.1038/s41467-021-21181-9},
  language = {eng},
}