Amyloids escape elimination by the proteasome, and their accumulation and subsequent aggregation contribute to various neurodegenerative conditions. A signature feature of amyloidogenic proteins is extended sequences rich in single amino acids. In this issue, Matouschek and colleagues now show that, to initiate degradation, the proteasome prefers substrates that have disordered regions with complex amino acid composition, thus indicating why it fails to rid the cell of most amyloids.
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Humbard, M., Maurizi, M. The proteasome gets a grip on protein complexity. Nat Struct Mol Biol 22, 181–183 (2015). https://doi.org/10.1038/nsmb.2977
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DOI: https://doi.org/10.1038/nsmb.2977
