The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The Control Centers of Biomolecular Phase Separation: How Membrane Surfaces, PTMs, and Active Processes Regulate Condensation
Open accessAbstract
Biomolecular condensation is emerging as an essential process for cellular compartmentalization. Formation of biomolecular condensates can be driven by liquid-liquid phase separation, which arises from weak, multivalent interactions among proteins and nucleic acids. A substantial body of recent work has revealed that diverse cellular processes rely on biomolecular condensation, and that aberrant phase separation may cause disease. Many proteins display an intrinsic propensity to undergo phase separation. However, the mechanisms by which cells regulate phase separation to build functional condensates at the appropriate time and location are only beginning to be understood. Here we review three key cellular mechanisms that enable control of biomolecular phase separation: membrane surfaces, post-translational modifications, and active processes. We discuss how these mechanisms may function in concert to provide robust control over biomolecular condensates, and suggest new research avenues that will elucidate how cells build and maintain these key centers of cellular compartmentalization.
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Cites
Lipid rafts as a membrane-organizing principle
Lingwood, D., & Simons, K. (2010) · Science · doi:10.1126/science.1174621 · Cited by 4,417
Nott, T. J., Petsalaki, E., Farber, P., Jervis, D., Fussner, E., Plochowietz, A., Craggs, T. D., Bazett-Jones, D. P., Pawson, T., Forman-Kay, J. D., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.01.013 · Cited by 1,803
Applying systems-level spectral imaging and analysis to reveal the organelle interactome
Valm, A. M., Cohen, S., Legant, W. R., Melunis, J., Hershberg, U., Wait, E., Cohen, A. R., Davidson, M. W., Betzig, E., & Lippincott-Schwartz, J. (2017) · Nature · doi:10.1038/nature22369 · Cited by 1,113
Südhof, T. C. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.012 · Cited by 1,062
Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782
Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779
Acetylation Disfavors Tau Phase Separation
Ferreon, J. C., Jain, A., Choi, K.-J., Tsoi, P. S., MacKenzie, K. R., Jung, S. Y., & Ferreon, A. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051360 · Cited by 183
Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics
Iversen, L., Tu, H.-L., Lin, W.-C., Christensen, S. M., Abel, S. M., Iwig, J., Wu, H.-J., Gureasko, J., Rhodes, C., Petit, R. S., et al. (2014) · Science · doi:10.1126/science.1250373 · Cited by 154
An acetylation–phosphorylation switch that regulates tau aggregation propensity and function
Carlomagno, Y., Chung, D.-E. C., Yue, M., Castanedes-Casey, M., Madden, B. J., Dunmore, J., Tong, J., DeTure, M., Dickson, D. W., Petrucelli, L., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.794602 · Cited by 143 · cited 8×
“Recent studies found that Tau phosphorylation alters the net charge and the charge distribution to promote electrostatic interactions that favor phase separation (Figure 3B; Ambadipudi et al., 2017; Wegmann et al., 2018), thereby helping to explain the formation of disease-linked Tau aggregates.”
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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 1,160
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Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 936
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Mitrea, D. M., Mittasch, M., Gomes, B. F., Klein, I. A., & Murcko, M. A. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00505-4 · Cited by 401
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Galvanetto, N., Ivanović, M. T., Chowdhury, A., Sottini, A., Nüesch, M. F., Nettels, D., Best, R. B., & Schuler, B. (2023) · Nature · doi:10.1038/s41586-023-06329-5 · Cited by 365
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Yu, H., Lu, S., Gasior, K., Singh, D., Vazquez-Sanchez, S., Tapia, O., Toprani, D., Beccari, M. S., Yates, J. R., Da Cruz, S., et al. (2021) · Science · doi:10.1126/science.abb4309 · Cited by 353
Self-citation
Metadata
- Authors
- Snead, W. T., & Gladfelter, A. S.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2019-10
- Volume
- 76
- Issue
- 2
- Pages
- 295-305
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2980184617
- Cited by
- 352
- References
- 9
- FWCI
- 10.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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