Cited by 1,278RNA Research and SplicingRNA and protein synthesis mechanismsProtein Structure and Dynamics

The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics

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Elbaum-Garfinkle, Shana, Kim, Younghoon, Szczepaniak, Krzysztof, Chen, Carlos Chih-Hsiung, Eckmann, Christian R., Myong, Sua, Brangwynne, Clifford P.·2015·Proceedings of the National Academy of Sciences

Abstract

Significance: Phase transitions have recently emerged as a key mechanism for intracellular organization. However, the underlying molecular interactions and nature of the resulting condensed phases are poorly understood. Here, we identify a role for LAF-1 in the liquid phase separation of P granules—RNA/protein assemblies implicated in germ-line maintenance. We adapt microrheology techniques to measure precise viscoelastic properties of LAF-1 liquid droplets. Our experiments reveal that electrostatic disordered protein interactions give rise to droplets with tunable material properties. RNA can fluidize protein droplets by decreasing the viscosity and increasing internal molecular dynamics. Our results provide insight into the mechanism by which molecular level interactions can give rise to liquid phase organelles with tunable material properties, potentially underlying biologically adaptable functions.

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  • Evidence for chromatin LLPS and its functional significance in gene control is still incomplete.

    “Whilst LLPS in general has been demonstrated both in vitro and in vivo [421, 422], evidence for chromatin LLPS and its functional significance in gene control is still incomplete.”

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Authors
Elbaum-Garfinkle, S., Kim, Y., Szczepaniak, K., Chen, C. C.-H., Eckmann, C. R., Myong, S., & Brangwynne, C. P.
Affiliations
  • Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08540;
  • University of Illinois Urbana-Champaign (US)
  • Max Planck Institute of Molecular Cell Biology and Genetics (DE)
  • Princeton University (US)
Venue
Proceedings of the National Academy of Sciences
Published
2015-05-26
Volume
112
Issue
23
Pages
7189-7194
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2111796925
Cited by
1,278
References
2
Citations by year
2026: 103 · 2025: 126 · 2024: 151 · 2023: 125 · 2022: 153 · 2021: 147 · 2020: 135 · 2019: 118 · 2018: 95 · 2017: 50 · 2016: 53 · 2015: 20
FWCI
31.57
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
  • Human Frontier Science Program (RGP0007/2012)
  • HHS | NIH | NIH Office of the Director (1DP2GM105437-01, 1DP2 GM105453 A)
  • Searle Scholars Program (12-SSP-217)
  • NSF (1253035)
  • American Cancer Society (RSG-12-066-01-DMC)
  • Deutsche Forschungsgemeinschaft (EC369-3/1)
  • Sachsen-Anhalt (EFRE start-up grant)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
P granules, intrinsically disordered proteins, phase separation, biomolecular condensates, viscoelasticity, droplet viscosity, RNA-protein interactions, microrheology, single-molecule FRET, Caenorhabditis elegans embryo, phase boundaries
MeSH terms
Animals, Viscosity, Caenorhabditis elegans, RNA, Helminth, RNA Helicases, Caenorhabditis elegans Proteins

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