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      Biomolecular condensates: organizers of cellular biochemistry.

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          Abstract

          Biomolecular condensates are micron-scale compartments in eukaryotic cells that lack surrounding membranes but function to concentrate proteins and nucleic acids. These condensates are involved in diverse processes, including RNA metabolism, ribosome biogenesis, the DNA damage response and signal transduction. Recent studies have shown that liquid-liquid phase separation driven by multivalent macromolecular interactions is an important organizing principle for biomolecular condensates. With this physical framework, it is now possible to explain how the assembly, composition, physical properties and biochemical and cellular functions of these important structures are regulated.

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          A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

          Avinash Patel, Hyun Lee, Louise M Jawerth … (2015)
          Many proteins contain disordered regions of low-sequence complexity, which cause aging-associated diseases because they are prone to aggregate. Here, we study FUS, a prion-like protein containing intrinsically disordered domains associated with the neurodegenerative disease ALS. We show that, in cells, FUS forms liquid compartments at sites of DNA damage and in the cytoplasm upon stress. We confirm this by reconstituting liquid FUS compartments in vitro. Using an in vitro "aging" experiment, we demonstrate that liquid droplets of FUS protein convert with time from a liquid to an aggregated state, and this conversion is accelerated by patient-derived mutations. We conclude that the physiological role of FUS requires forming dynamic liquid-like compartments. We propose that liquid-like compartments carry the trade-off between functionality and risk of aggregation and that aberrant phase transitions within liquid-like compartments lie at the heart of ALS and, presumably, other age-related diseases.
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            Liquid-liquid phase separation in biology.

            Anthony Hyman, Christoph Weber, Frank Jülicher (2014)
            Cells organize many of their biochemical reactions in non-membrane compartments. Recent evidence has shown that many of these compartments are liquids that form by phase separation from the cytoplasm. Here we discuss the basic physical concepts necessary to understand the consequences of liquid-like states for biological functions.
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              Germline P granules are liquid droplets that localize by controlled dissolution/condensation.

              Clifford Brangwynne, Christian R. Eckmann, David S Courson … (2009)
              In sexually reproducing organisms, embryos specify germ cells, which ultimately generate sperm and eggs. In Caenorhabditis elegans, the first germ cell is established when RNA and protein-rich P granules localize to the posterior of the one-cell embryo. Localization of P granules and their physical nature remain poorly understood. Here we show that P granules exhibit liquid-like behaviors, including fusion, dripping, and wetting, which we used to estimate their viscosity and surface tension. As with other liquids, P granules rapidly dissolved and condensed. Localization occurred by a biased increase in P granule condensation at the posterior. This process reflects a classic phase transition, in which polarity proteins vary the condensation point across the cell. Such phase transitions may represent a fundamental physicochemical mechanism for structuring the cytoplasm.
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                Author and article information

                Journal
                Journal ID (iso-abbrev): Nat. Rev. Mol. Cell Biol.
                Title: Nature reviews. Molecular cell biology
                Publisher: Springer Nature
                ISSN (Electronic): 1471-0080
                ISSN (Print): 1471-0072
                Publication date (Electronic): May 2017
                Volume: 18
                Issue: 5
                Affiliations
                [1 ] Department of Biophysics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA.
                [2 ] Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
                Article
                Publisher Item ID: nrm.2017.7
                DOI: 10.1038/nrm.2017.7
                PubMed ID: 28225081
                SO-VID: d1ceaa65-aeb1-4aca-a3b5-6f47d96dfd7b
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