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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.

ABSTRACT: 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.

SUBMITTER: Krainer G

PROVIDER: S-EPMC7889641 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.

Krainer Georg G Welsh Timothy J TJ Joseph Jerelle A JA Espinosa Jorge R JR Wittmann Sina S de Csilléry Ella E Sridhar Akshay A Toprakcioglu Zenon Z Gudiškytė Giedre G Czekalska Magdalena A MA Arter William E WE Guillén-Boixet Jordina J Franzmann Titus M TM Qamar Seema S George-Hyslop Peter St PS Hyman Anthony A AA Collepardo-Guevara Rosana R Alberti Simon S Knowles Tuomas P J TPJ

Nature communications 20210217 1

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 togethe ...[more]

PMID: 33597515

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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.

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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions.

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