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Ubiquitin protein helps cells to recover from stress

In stressed cells, proteins and RNA molecules cluster together to form stress granules. It emerges that the small protein modifier ubiquitin is needed to disassemble stress granules in recovering cells.
  1. Titus Franzmann

    1. Titus Franzmann is at the Biotechnology Center, Center for Molecular and Cellular Bioengineering, Technische Universität Dresden, 01307 Dresden, Germany.

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  2. Simon Alberti

    1. Simon Alberti is at the Biotechnology Center, Center for Molecular and Cellular Bioengineering, Technische Universität Dresden, 01307 Dresden, Germany.

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The biggest threat to a cell during exposure to environmental stress factors, such as high temperature, is the unfolding of its proteins. Two strategies prevent the accumulation of damaged proteins: refolding, which is assisted by chaperone proteins, and protein degradation. In one degradation pathway, ubiquitin molecules are attached to target proteins to signal that they are to be degraded by a protein complex called the proteasome. Early work showed that heat stress induces the ubiquitination and proteasomal degradation of cellular proteins1. Now, writing in Science, Maxwell et al.2 and Gwon et al.3 report that ubiquitination of a large set of proteins is required to recover normal cellular function when stress subsides.

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Nature 597, 183-184 (2021)

doi: https://doi.org/10.1038/d41586-021-02197-z

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Competing Interests

S.A. is a scientific adviser of Dewpoint Therapeutics.

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