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PROTEIN AGGREGATION

Amyloids as kinase signalling platforms

Nature Reviews Molecular Cell Biology volume 24, page 85 (2023)Cite this article

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Amyloids are the best-known higher-order protein structures, forming distinct rigid fibrils. They were originally defined as a unique form of protein folding disorder, which leads to unspecific cellular dysfunction in many diseases, in particular neurodegenerative disorders. Ironically, these ‘disordered’ protein aggregates feature a central cross-β spine, with solvent-excluded, self-complementing steric zipper interactions, thereby sharing the core characteristics of ‘highly ordered’ cross-β-sheet packing. Is the beauty of these rigid fibrils merely awry bug of nature? Intriguingly, amyloids were also found to contribute to signal transduction in human. In 2012, Li et al. revealed the amyloidal nature of a class of cytosolic RHIM-containing kinases, RIPK1 and RIPK3. With this discovery, a novel amyloidal kinase-mediated signalling transduction rose into view.

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Original article

  • Li, J. et al. The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. Cell 150, 339–350 (2012)

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  1. Center for Excellence in Molecular Cell Science, Chinese Academy of Sciences, Shanghai, China

    Liming Sun

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  1. Liming Sun
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Correspondence to Liming Sun.

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Sun, L. Amyloids as kinase signalling platforms. Nat Rev Mol Cell Biol 24, 85 (2023). https://doi.org/10.1038/s41580-022-00553-z

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  • DOI: https://doi.org/10.1038/s41580-022-00553-z

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