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A chloroplast proteostasis factor prevents aggregation of a human disease-related protein

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Plants have an additional organelle to animals (the chloroplast), which means that they have a greater repertoire of protein homeostasis (proteostasis) mechanisms. We find that chloroplast proteostasis components prevent aggregation of a pathogenic fragment of human huntingtin expressed in plants, which reveals a potential avenue for therapeutic intervention in human proteinopathies.

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Fig. 1: PolyQ-expanded mutant huntingtin aggregation in plants and human cells.

References

  1. Pérez-Llorca, M. & Munné-Bosch, S. Aging, stress, and senescence in plants: what can biological diversity teach us? GeroScience 43, 167–180 (2021). A review that discusses plant longevity and the underlying mechanisms.

    PubMed  PubMed Central  Google Scholar 

  2. Jung, J. H. et al. A prion-like domain in ELF3 functions as a thermosensor in Arabidopsis. Nature 585, 256–260 (2020). This paper reports that aggregation of the transcription factor EARLY FLOWERING 3 (ELF3) containing a Q7 stretch enables plants to respond to high temperatures.

    CAS  PubMed  Google Scholar 

  3. Dorone, Y. et al. A prion-like protein regulator of seed germination undergoes hydration-dependent phase separation. Cell. 184, 4284–4298 (2021). This paper reports a plant prion-like protein that phase separates on hydration and thereby serves as a water stress sensor in embryos.

    CAS  PubMed  PubMed Central  Google Scholar 

  4. Rowland, E. et al. The CLP and PREP protease systems coordinate maturation and degradation of the chloroplast proteome in Arabidopsis thaliana. New Phytol. 236, 1339–1357 (2022). This paper reports that SPP is upregulated and binds to unstructured peptides to counteract the loss of chaperone capacity in plants.

    CAS  PubMed  Google Scholar 

  5. Lieberman, A. P. et al. Polyglutamine repeats in neurodegenerative diseases. Annu. Rev. Pathol. 14, 1–27 (2018). A review that provides an overview of the nine human neurodegenerative diseases caused by aggregation of polyQ-expanded proteins.

    PubMed  PubMed Central  Google Scholar 

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This is a summary of: Llamas, E. et al. In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation. Nat. Plants, https://doi.org/10.1038/s43587-023-00502-1 (2023).

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A chloroplast proteostasis factor prevents aggregation of a human disease-related protein. Nat Aging 3, 1323–1324 (2023). https://doi.org/10.1038/s43587-023-00503-0

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