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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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“The process of LLPS is favored by multivalent interactions between specific protein domains, intrinsically disordered regions in proteins (IDR) and nucleic acids [4].”
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“This latter finding was unexpected since PML bodies are membraneless structures that are formed in an aqueous environment [36,37].”
BackgroundMATR3‐antisense LINE1 RNA meshwork scaffolds higher‐order chromatin organization
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“Recent studies have revealed dynamic nuclear compartments driven by the liquid – liquid phase separation (LLPS) of proteins and/ or RNAs (Stanek & Fox, 2017; Lyon et al , 2021).”
Phase separation of YAP-MAML2 differentially regulates the transcriptome
Chung, C.-I., Yang, J., Yang, X., Liu, H., Ma, Z., Szulzewsky, F., Holland, E. C., Shen, Y., & Shu, X. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310430121 · Cited by 22
Nucleoporin Nsp1 surveils the phase state of FG-Nups
Otto, T. A., Bergsma, T., Dekker, M., Mouton, S. N., Gallardo, P., Wolters, J. C., Steen, A., Onck, P. R., & Veenhoff, L. M. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114793 · Cited by 24
Recent advances in design and application of synthetic membraneless organelles
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Phosphorylation-dependent charge blocks regulate the relaxation of nuclear speckle networks
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Membranes regulate biomolecular condensates
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Micellization: A new principle in the formation of biomolecular condensates
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Hyperstabilization of T cell microvilli contacts by chimeric antigen receptors
Beppler, C., Eichorst, J. P., Marchuk, K., Cai, E., Castellanos, C. A., Sriram, V., Roybal, K. T., & Krummel, M. F. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202205118 · Cited by 20
“Given the allowance for variable-sized patches used in this analysis, the patches we refer to may encompass multiple types of accumulations, such as from “ condensates ” (Lyon et al., 2021) or random fluctuations.”
MethodGenetic switches based on nucleic acid strand displacement
Wang, T., Hellmer, H., & Simmel, F. C. (2022) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2022.102867 · Cited by 20
Cell surface-localized CsgF condensate is a gatekeeper in bacterial curli subunit secretion
Swasthi, H. M., Basalla, J. L., Dudley, C. E., Vecchiarelli, A. G., & Chapman, M. R. (2023) · Nature Communications · doi:10.1038/s41467-023-38089-1 · Cited by 19
“Proteins that are associated with neurode-generativediseases,suchasTau,TDP-43,andFUS,havethepropensity to undergo phase separation and to aggregate within the droplets 44,45,66 .”
Involvement of small molecules and metabolites in regulation of biomolecular condensate properties
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Chemogenetic Minitool for Dissecting the Roles of Protein Phase Separation
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Self-consistent sharp interface theory of active condensate dynamics
Goychuk, A., Demarchi, L., Maryshev, I., & Frey, E. (2024) · Physical Review Research · doi:10.1103/physrevresearch.6.033082 · Cited by 20
“The underlying mechanism, where a liquid mixture phase separates according to differences in the interactions among its components, enables condensates to naturally buffer molecules [8] and compartmentalize reactions [4].”
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“Homo-FRET, like heteroFRET, serves as a nanometric proximity ruler (2 – 10nm), but with an additional prerequisite of a small Stokes ’ shift permitting a spectral overlap between the absorption and emission spectra of the fl uorophore.”
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Separation of sticker-spacer energetics governs the coalescence of metastable condensates
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Nanoscale domains govern local diffusion and ageing within fused-in-sarcoma condensates
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“These condensates selectively recruit RNA molecules and their processing machineries 1,3,5–7 , providing a distinct biochemical environment that either enhances reaction rates or suppresses processing 8,9 .”
Regulation of the activity of the bacterial histidine kinase PleC by the scaffolding protein PodJ
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“m AU Size exclusion chromatography PodJ(1-635)”
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Emerging Mechanisms of Skeletal Muscle Homeostasis and Cachexia: The SUMO Perspective
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“The SUMO pathway acts as a molecular stress sensor and plays a key role in a process known as liquid–liquid phase separation (LLPS), which generates bio-molecular condensates or membrane-less organelles [89,90].”
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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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