Cited by 901RNA Research and SplicingNuclear Structure and FunctionGenomics and Chromatin Dynamics

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A framework for understanding the functions of biomolecular condensates across scales

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Lyon, Andrew S., Peeples, William B., Rosen, Michael K.·2021·Nature Reviews Molecular Cell Biology

DOI 10.1038/s41580-020-00303-zPMC PMC8574987

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Abstract

Biomolecular condensates are found throughout eukaryotic cells, including in the nucleus, in the cytoplasm and on membranes. They are also implicated in a wide range of cellular functions, organizing molecules that act in processes ranging from RNA metabolism to signalling to gene regulation. Early work in the field focused on identifying condensates and understanding how their physical properties and regulation arise from molecular constituents. Recent years have brought a focus on understanding condensate functions. Studies have revealed functions that span different length scales: from molecular (modulating the rates of chemical reactions) to mesoscale (organizing large structures within cells) to cellular (facilitating localization of cellular materials and homeostatic responses). In this Roadmap, we discuss representative examples of biochemical and cellular functions of biomolecular condensates from the recent literature and organize these functions into a series of non-exclusive classes across the different length scales. We conclude with a discussion of areas of current interest and challenges in the field, and thoughts about how progress may be made to further our understanding of the widespread roles of condensates in cell biology.

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Additional file 2 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Additional file 3 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Additional file 11 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Additional file 9 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Additional file 8 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Additional file 7 of Investigating phase separation properties of chromatin-associated proteins using gradient elution of 1,6-hexanediol
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Mori, M., Sugai, H., Sato, K., Okada, A., Matsuo, T., & Kinbara, K. (2024) · Chemical Communications · doi:10.1039/d4cc01117a
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Koyuncu, A. H., Allegri, G., Moazzenzade, T., Huskens, J., Lindhoud, S., & Wong, A. S. Y. (2024) · ChemSystemsChem · doi:10.1002/syst.202400050
Recombinant silk protein condensates show widely different properties depending on the sample background
Tersteegen, J., Tunn, I., Sand, M., Välisalmi, T., Malkamäki, M., Gandier, J., Beaune, G., Sanz-Velasco, A., Anaya‐Plaza, E., & Linder, M. B. (2024) · Journal of Materials Chemistry B · doi:10.1039/d4tb01422g
Epigenetic silencing and blockade of latency reversal by an HIV-1 encoded antisense transcriptPreprint
Li, R., Daneshvar, K., Ji, X., Pleet, M. L., Igbinosun, G., Iqbal, M. S., Kashanchi, F., Mullen, A. C., & Romerio, F. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.06.627241
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Koslover, E. F. (2024) · Springer eBooks · doi:10.1007/978-3-031-67802-8_22
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Lin, Y.-H., Kim, T. H., Das, S., Pal, T., Wessén, J., Rangadurai, A., Kay, L. E., Forman-Kay, J. D., & Chan, H. S. (2024) · eLife · doi:10.7554/elife.100284.2
Image-based screens identify regulators of endogenous Dvl2 biomolecular condensatesPreprint
Schubert, A., Heigwer, F., Scheeder, C., Voloshanenko, O., Kranz, D., Ragaller, F., Winkler, N., Miersch, T., Schmitt, B. A., Kuhse, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.11.632522
Toward universal models for collective interactions in biomolecular condensates
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A synthetic biomolecular condensate from plant proteins with controlled colloidal properties
Ghosh, P., Buhaichuk, N., Carr, J., Tani, S., Hazra, R. S., Mathew, S., Choi, Y., & Quadir, M. (2025) · Journal of Materials Chemistry B · doi:10.1039/d5tb00137d
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Cornwall, G. A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-21477-6.00456-9
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Polyansky, A. A., Frühbauer, B., & Žagrović, B. (2026) · Communications Chemistry · doi:10.1038/s42004-026-01974-z
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Roy, S. (2025) · Springer eBooks · doi:10.1007/978-981-96-6823-6_6 · Cited by 1
Solvent Pre and Effective Near Surface Electrostatics: Theory, Methods, and Biological InsightsPreprint
Okuno, Y., & Griggs, S. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5383586
Transport kinetics across interfaces between coexisting liquid phasesPreprint
Hubatsch, L., Bo, S., Harmon, T. S., Hyman, A. A., Weber, C. A., & Jülicher, F. (2025) · eLife · doi:10.7554/elife.106842
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“Condensates can coordinate versatile cellular processes, e.g., gene regulation, signaling and stress response (2, 5, 9, 10), and each process involves various activities of condensate like storage of biomolecules and wetting with membrane structures (9, 11-16).”
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HAND2 invades nucleolar condensates to pioneer lineage-specific cardiac pacemaker gene programs
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“To corroborate an effect on “gene programs” the analysis should contain information about a larger number of PM and sarcomeric marker genes and their dependency on HAND2 nucleolar localization.”
Paralogs with distinct phase behaviors broaden the in vivo stress response range of condensatesPreprint
Guan, J., Sahoo, B. R., Brant, T. S., Mahadevan, P., Brooks, A., Mosalaganti, S., Bardwell, J. C. A., & Jakob, U. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.13.682129
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Zuo, L., Guo, Q., Li, C., Zhang, K., Chen, Y., Jiang, B., Chen, Z., Xia, Y., Qian, L., Zhang, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65069-4 · Cited by 2
“1 and 9) were performed to test the binding af ﬁ nity of proteins-DNA.”
Biomolecules’ mutations and physical disorders modulating life’s processes
Ashrafuzzaman, M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-36368-9.00016-0

Authors: Lyon, A. S., Peeples, W. B., & Rosen, M. K.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Rosen, Michael K.
ORCID: Lyon, Andrew S.
Peeples, William B.
Rosen, Michael K.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2020-11-09
Volume: 22
Issue: 3
Pages: 215-235
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/s41580-020-00303-z
PMC: PMC8574987
OpenAlex: W3099323319
Cited by: 895
References: 233
Citations by year: 2026: 149 · 2025: 186 · 2024: 175 · 2023: 172 · 2022: 115 · 2021: 95 · 2020: 2
FWCI: 9.35
Type: journal article
Language: en
Open access: green
europepmc.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature Reviews Molecular Cell Biology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: Howard Hughes Medical Institute
National Institute of General Medical Sciences (F32GM136058)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: biomolecular condensates, liquid-liquid phase separation, length scales, RNA metabolism, gene expression regulation, cell organization, signal transduction, reaction rate, cellular homeostasis
MeSH terms: Animals, Biochemical Phenomena, Cell Physiological Phenomena, Cytoplasm, Eukaryotic Cells, Humans, Organelles, Macromolecular Substances, Multiprotein Complexes, Protein Aggregates

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A framework for understanding the functions of biomolecular condensates across scales

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