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PHASE SEPARATION

Protein quality and miRNA slicing get into phase

Nature Cell Biology volume 20, pages 635–637 (2018)Cite this article

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Phase separation can build assemblies and regulate biological function. Two articles link specific forms of protein and RNA degradation to phase separation. The polyubiquitin shuttle factor UBQLN2 localizes to stress granules where it may extract ubiquitinated proteins, and the miRISC complex functions through phase separation.

Liquid–liquid phase separation (LLPS) mediates the condensation of proteins and nucleic acids into dense liquid droplets, and has recently been recognized as a key mechanism underlying the formation of membrane-less organelles such as stress granules, P bodies and the nucleolus in cells. Importantly, studies of LLPS have revealed new mechanistic insights into the pathophysiology of neurodegenerative diseases because disease-associated aggregation processes are enhanced in dense phases. These new concepts have led to a paradigm-shift in our understanding of subcellular compartmentalization1. Two recent articles illustrate how the cellular machinery specifying both mRNA and protein degradation can function in phase-separated bodies2,3.

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Affiliations

  1. Department of Structural Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA

    Tanja Mittag

  2. Department of Molecular Pharmacology, Physiology, and Biotechnology, Brown University, Providence, RI, USA

    Nicolas L. Fawzi

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  1. Tanja Mittag
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  2. Nicolas L. Fawzi
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Correspondence to Tanja Mittag or Nicolas L. Fawzi.

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The authors declare no competing interests.

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Cite this article

Mittag, T., Fawzi, N.L. Protein quality and miRNA slicing get into phase. Nat Cell Biol 20, 635–637 (2018). https://doi.org/10.1038/s41556-018-0113-4

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  • DOI: https://doi.org/10.1038/s41556-018-0113-4

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