Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, which form condensates at low...
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2021
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oai:doaj.org-article:f1a7c13511ed46d3b7d48b9f4017a81c2021-12-02T12:11:27ZReentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions10.1038/s41467-021-21181-92041-1723https://doaj.org/article/f1a7c13511ed46d3b7d48b9f4017a81c2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21181-9https://doaj.org/toc/2041-1723Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, which form condensates at low salt concentrations, can reenter a phase-separated regime at high salt concentrations.Georg KrainerTimothy J. WelshJerelle A. JosephJorge R. EspinosaSina WittmannElla de CsilléryAkshay SridharZenon ToprakciogluGiedre GudiškytėMagdalena A. CzekalskaWilliam E. ArterJordina Guillén-BoixetTitus M. FranzmannSeema QamarPeter St George-HyslopAnthony A. HymanRosana Collepardo-GuevaraSimon AlbertiTuomas P. J. KnowlesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021) |
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Science Q Georg Krainer Timothy J. Welsh Jerelle A. Joseph Jorge R. Espinosa Sina Wittmann Ella de Csilléry Akshay Sridhar Zenon Toprakcioglu Giedre Gudiškytė Magdalena A. Czekalska William E. Arter Jordina Guillén-Boixet Titus M. Franzmann Seema Qamar Peter St George-Hyslop Anthony A. Hyman Rosana Collepardo-Guevara Simon Alberti Tuomas P. J. Knowles Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
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Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, which form condensates at low salt concentrations, can reenter a phase-separated regime at high salt concentrations. |
format |
article |
author |
Georg Krainer Timothy J. Welsh Jerelle A. Joseph Jorge R. Espinosa Sina Wittmann Ella de Csilléry Akshay Sridhar Zenon Toprakcioglu Giedre Gudiškytė Magdalena A. Czekalska William E. Arter Jordina Guillén-Boixet Titus M. Franzmann Seema Qamar Peter St George-Hyslop Anthony A. Hyman Rosana Collepardo-Guevara Simon Alberti Tuomas P. J. Knowles |
author_facet |
Georg Krainer Timothy J. Welsh Jerelle A. Joseph Jorge R. Espinosa Sina Wittmann Ella de Csilléry Akshay Sridhar Zenon Toprakcioglu Giedre Gudiškytė Magdalena A. Czekalska William E. Arter Jordina Guillén-Boixet Titus M. Franzmann Seema Qamar Peter St George-Hyslop Anthony A. Hyman Rosana Collepardo-Guevara Simon Alberti Tuomas P. J. Knowles |
author_sort |
Georg Krainer |
title |
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
title_short |
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
title_full |
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
title_fullStr |
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
title_full_unstemmed |
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
title_sort |
reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/f1a7c13511ed46d3b7d48b9f4017a81c |
work_keys_str_mv |
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