ArticleNature chemical biology2020
Designer protein assemblies with tunable phase diagrams in living cells.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 105 citations in OpenAlex.
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- Design and applications of synthetic biomolecular condensates.Nature nanotechnology · 2026Review
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- Toward Design Principles for Biomolecular Condensates for Metabolic Pathways.Advanced biology · 2025Review
- Uncovering the mechanism for polar sequestration of the major bacterial sugar regulator by high-throughput screens and 3D interaction modeling.Cell reports · 2025Article
- Molecular determinants of condensate composition.Molecular cell · 2025Review
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- Dominance analysis to assess solute contributions to multicomponent phase equilibria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Surface Charge Can Modulate Phase Separation of Multidomain Proteins.Journal of the American Chemical Society · 2024Article
- Assembling membraneless organelles from de novo designed proteins.Nature chemistry · 2024Article
- Liquid-liquid phase separation driven by charge heterogeneity.Communications physics · 2024Article
- Programmable de novo designed coiled coil-mediated phase separation in mammalian cells.Nature communications · 2023Article
- Agglomeration: when folded proteins clump together.Biophysical reviews · 2023Review
- Dynamical control enables the formation of demixed biomolecular condensates.Nature communications · 2023Article
- Condensate functionalization with microtubule motors directs their nucleation in space and allows manipulating RNA localization.The EMBO journal · 2023Article
- Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans.Communications biology · 2023Article
- Chemogenetic Minitool for Dissecting the Roles of Protein Phase Separation.ACS central science · 2023Article
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Authors and funding
11 authors at 4 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein self-organization is a hallmark of biological systems. Although the physicochemical principles governing protein-protein interactions have long been known, the principles by which such nanoscale interactions generate diverse phenotypes of mesoscale assemblies, including phase-separated compartments, remain challenging to characterize. To illuminate such principles, we create a system of two proteins designed to interact and form mesh-like assemblies. We devise a new strategy to map high-resolution phase diagrams in living cells, which provide self-assembly signatures of this system. The structural modularity of the two protein components allows straightforward modification of their molecular properties, enabling us to characterize how interaction affinity impacts the phase diagram and material state of the assemblies in vivo. The phase diagrams and their dependence on interaction affinity were captured by theory and simulations, including out-of-equilibrium effects seen in growing cells. Finally, we find that cotranslational protein binding suffices to recruit a messenger RNA to the designed micron-scale structures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.