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- Maarten Hardenberg
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom;
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- Attila Horvath
- The John Curtin School of Medical Research, The Australian National University, Canberra, ACT 2601, Australia;
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- Viktor Ambrus
- Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, H-4010 Debrecen, Hungary;
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- Monika Fuxreiter
- Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, H-4010 Debrecen, Hungary;
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- Michele Vendruscolo
- Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom;
説明
<jats:title>Significance</jats:title> <jats:p>Liquid–liquid phase separation of proteins results in biomolecular condensates, which contribute to the organization of cellular matter into membraneless organelles. It is still unclear, however, whether these condensates represent a common state of proteins. Here, based on biophysical principles driving phase separation, we report a proteome-wide ranking of proteins according to their propensity to condensate into a droplet state. We analyze two mechanisms for droplet formation—driver proteins can spontaneously phase separate, while client proteins require additional components. We conclude that the droplet state, as the native and amyloid states, is a fundamental state of proteins, with most proteins expected to be capable of undergoing liquid–liquid phase separation via either of these two mechanisms.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 117 (52), 33254-33262, 2020-12-14
Proceedings of the National Academy of Sciences
