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A framework for understanding the functions of biomolecular condensates across scales
Open accessAbstract
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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“The second systems biology criterion follows from the observation that integrated function is only possible via structured spatial heterogeneity, that is, that spatial heterogeneity is crucial to cellular function.”
From ‘Whole Organism’, Systems Biology, and Top-Down Criteria for Evaluating Scenarios for the Origin of Life (2021) · cites this paper as [45]
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Cites
Items 201–237 of 237
Liquid–liquid phase separation of the Golgi matrix protein GM130
Rebane, A. A., Ziltener, P., LaMonica, L. C., Bauer, A. H., Zheng, H., López‐Montero, I., Pincet, F., Rothman, J. E., & Ernst, A. M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13715 · Cited by 79
Inhibition of synucleinopathic seeding by rationally designed inhibitors
Sangwan, S., Sahay, S., Murray, K. A., Morgan, S., Guenther, E. L., Jiang, L., Williams, C. K., Vinters, H. V., Goedert, M., & Eisenberg, D. S. (2020) · eLife · doi:10.7554/elife.46775 · Cited by 79
A Non-amyloid Prion Particle that Activates a Heritable Gene Expression Program
Chakravarty, A. K., Smejkal, T., Itakura, A. K., Garcia, D. M., & Jarosz, D. F. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.028 · Cited by 77
Phase separation of Polo-like kinase 4 by autoactivation and clustering drives centriole biogenesis
Park, J., Zhang, L., Bang, J. K., Andrésson, Þ., DiMaio, F., & Lee, K. S. (2019) · Nature Communications · doi:10.1038/s41467-019-12619-2 · Cited by 72
Constraints and consequences of the emergence of amino acid repeats in eukaryotic proteins
Chavali, S., Chavali, P. L., Chalancon, G., de Groot, N. S., Gemayel, R., Latysheva, N. S., Ing‐Simmons, E., Verstrepen, K. J., Santhanam, B., & Babu, M. M. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3441 · Cited by 68
Asymmetric mRNA localization contributes to fidelity and sensitivity of spatially localized systems
Weatheritt, R. J., Gibson, T. J., & Babu, M. M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2876 · Cited by 61
Aurora A activation in mitosis promoted by BuGZ
Huang, Y., Li, T., Ems-McClung, S. C., Walczak, C., Prigent, C., Zhu, X., Zhang, X., & Zheng, Y. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201706103 · Cited by 49
A guide to regulation of the formation of biomolecular condensates
Bratek‐Skicki, A., Pancsa, R., Mészáros, B., Lindt, J. V., & Tompa, P. (2020) · FEBS Journal · doi:10.1111/febs.15254 · Cited by 48
Samaddar, M. (2019) · doi:10.1242/prelights.13626 · Cited by 47
Küffner, A. M., Prodan, M., Zuccarini, R., Palmiero, U. C., Faltova, L., & Arosio, P. (2020) · ChemSystemsChem · doi:10.1002/syst.202000027 · Cited by 45
Widespread Prion-Based Control of Growth and Differentiation Strategies in Saccharomyces cerevisiae
Itakura, A. K., Chakravarty, A. K., Jakobson, C. M., & Jarosz, D. F. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.10.027 · Cited by 42
The ERC1 scaffold protein implicated in cell motility drives the assembly of a liquid phase
Sala, K., Corbetta, A., Minici, C., Tonoli, D., Murray, D. H., Cammarota, E., Ribolla, L. M., Ramella, M., Fesce, R., Mazza, D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-49630-y · Cited by 41
Davis, D., Yuan, H., Liang, F., Yang, Y., Westley, J., Petzold, C., Dancel-Manning, K., Deng, Y., Sall, J., & Sehgal, P. B. (2019) · Journal of Virology · doi:10.1128/jvi.01014-19 · Cited by 40
Discovery Stories of RET Fusions in Lung Cancer: A Mini-Review
Takeuchi, K. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00216 · Cited by 39
CO 2 ‐fixing liquid droplets: Towards a dissection of the microalgal pyrenoid
Wunder, T., Oh, Z. G., & Mueller‐Cajar, O. (2019) · Traffic · doi:10.1111/tra.12650 · Cited by 39
Julin, J., Napari, I., Merikanto, J., & Vehkamäki, H. (2010) · The Journal of Chemical Physics · doi:10.1063/1.3456184 · Cited by 33
Tubulo‐interstitial disease in lupus nephritis. A morphometric study
Magil, A. B., & Tyler, M. G. (1984) · Histopathology · doi:10.1111/j.1365-2559.1984.tb02324.x · Cited by 33
Measurement of the Curvature-Dependent Surface Tension in Nucleating Colloidal Liquids
Nguyen, V. D., Schoemaker, F. C., Blokhuis, E. M., & Schall, P. (2018) · Physical Review Letters · doi:10.1103/physrevlett.121.246102 · Cited by 28
Phase Separation Can Increase Enzyme Activity by Concentration and Molecular OrganizationPreprint
Peeples, W. B., & Rosen, M. K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.15.299115 · Cited by 23
Self-citationA Carbonic Anhydrase Pseudogene Sensitizes Select Brucella Lineages to Low CO 2 Tension
Varesio, L. M., Willett, J. W., Fiebig, A., & Crosson, S. (2019) · Journal of Bacteriology · doi:10.1128/jb.00509-19 · Cited by 20
On the fine structure of the perivascular cells in the neural lobe of rats
Olivieri-Sangiacomo, C. (1972) · Cell and Tissue Research · doi:10.1007/bf00310294 · Cited by 19
Water droplet excess free energy determined by cluster mitosis using guided molecular dynamics
Lau, G. V., Hunt, P. A., Müller, E. A., Jackson, G., & Ford, I. J. (2015) · The Journal of Chemical Physics · doi:10.1063/1.4935198 · Cited by 19
Bergeron-Sandoval, L., Heris, H. K., Chang, C., Cornell, C., Keller, S., François, P., Hendricks, A. G., Ehrlicher, A. J., Pappu, R., & Michnick, S. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/145664 · Cited by 19
Certification Requirements of General Educators concerning Exceptional Pupils
Smith, J. E., & Schindler, W. J. (1980) · Exceptional Children · doi:10.1177/001440298004600511 · Cited by 19
The fitness cost and benefit of phase‐separated protein deposits
de Groot, N. S., Torrent, M., Ravarani, C. N. J., Trusina, A., Ventura, S., & Babu, M. M. (2019) · Molecular Systems Biology · doi:10.15252/msb.20178075 · Cited by 15
Thermodynamics and Statistical Mechanics of Small Systems
Puglisi, A., Sarracino, A., & Vulpiani, A. (2018) · Entropy · doi:10.3390/e20060392 · Cited by 14
Dense Bicoid Hubs Accentuate Binding along the Morphogen GradientPreprint
Mir, M., Reimer, A. E., Haines, J. E., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/133124 · Cited by 12
Nishimura, T., Yamaguchi, O., Takatani, N., Maeda, S.-I., & Omata, T. (2014) · Photosynthesis Research · doi:10.1007/s11120-014-9986-7 · Cited by 11
Both G3BP1 and G3BP2 contribute to stress granule formation
松木, 秀. (2013) · Medical Entomology and Zoology · Cited by 11
[Cyclophosphan and prednisolone immunosuppressant therapy of a patient with hypoplastic anemia].
Tn, P., Bv, A., Zaritskiĭ, A. I., Saĭdali, M. A., & Ts, Z. (1980) · PubMed · Cited by 8
Kinase-Mediated RAS Signaling Via Membraneless Cytoplasmic Protein GranulesPreprint
Tulpule, A., Guan, J., Neel, D. S., et al. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3578156 · Cited by 7
Correlative live and super-resolution imaging reveals the dynamic structure of replication domainsPreprint
Xiang, W., Roberti, M. J., Hèriché, J.-K., et al. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/189373 · Cited by 5
Tibble, R. W., Depaix, A., Kowalska, J., Jemielity, J., & Gross, J. (2020) · bioRxiv · doi:10.1101/2020.07.09.195057 · Cited by 5
Cioli, S., Mazzilli, G., Nizzola, G. M., & Panagis, P. (1969) · PubMed · Cited by 4
Incisor crowding and serial extraction.
Jb, J. (1981) · PubMed · Cited by 2
The fitness cost and benefit of phase separated protein depositsPreprint
de Groot, N. S., Torrent, M., Ravarani, C. N. J., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/574657 · Cited by 2
Prospective epidemiological study of arterial hypertension under preventive measures.
Kv, M., & YuV, S. (1986) · PubMed · Cited by 1
Cited by
Sorted by citations
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing
Alberti, S., & Hyman, A. A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00326-6 · Cited by 1,165
The molecular basis for cellular function of intrinsically disordered protein regions
Holehouse, A. S., & Kragelund, B. B. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00673-0 · Cited by 741
“The physical principles underlying phase transitions in biology have been reviewed extensively elsewhere 140,301–305 , as has the form and function of biomolecular condensates 296,300,306,307 .”
Signalling mechanisms and cellular functions of SUMO
Vertegaal, A. C. O. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00500-y · Cited by 394
CLIP and complementary methods
Hafner, M., Katsantoni, M., Köster, T., Marks, J., Mukherjee, J., Staiger, D., Ule, J., & Zavolan, M. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-021-00018-1 · Cited by 406
Bao, H., Cao, J., Chen, M., Min, C., Chen, W., Chen, X., Chen, Y., Chen, Y., Chen, Y., Chen, Z., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-023-2305-0 · Cited by 402
Metadata
- Authors
- Lyon, A. S., Peeples, W. B., & Rosen, M. K.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Rosen, Michael K.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2020-11-09
- Volume
- 22
- Issue
- 3
- Pages
- 215-235
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- 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
- 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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