Nature Communications (Feb 2021)
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
- 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
Affiliations
- Georg Krainer
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Timothy J. Welsh
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Jerelle A. Joseph
- Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue
- Jorge R. Espinosa
- Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue
- Sina Wittmann
- Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG)
- Ella de Csilléry
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Akshay Sridhar
- Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue
- Zenon Toprakcioglu
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Giedre Gudiškytė
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Magdalena A. Czekalska
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- William E. Arter
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- Jordina Guillén-Boixet
- Biotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universität Dresden, Tatzberg 47/49
- Titus M. Franzmann
- Biotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universität Dresden, Tatzberg 47/49
- Seema Qamar
- Cambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge
- Peter St George-Hyslop
- Cambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge
- Anthony A. Hyman
- Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG)
- Rosana Collepardo-Guevara
- Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue
- Simon Alberti
- Biotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universität Dresden, Tatzberg 47/49
- Tuomas P. J. Knowles
- Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge
- DOI
- https://doi.org/10.1038/s41467-021-21181-9
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 14
Abstract
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.
