Protein thermal sensing regulates physiological amyloid aggregation

Dane Marijan, Evgenia A. Momchilova, Daniel Burns, Sahil Chandhok, Richard Zapf, Holger Wille, Davit A. Potoyan and Timothy E. Audas ()
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Dane Marijan: Simon Fraser University
Evgenia A. Momchilova: Simon Fraser University
Daniel Burns: Iowa State University
Sahil Chandhok: Simon Fraser University
Richard Zapf: Simon Fraser University
Holger Wille: University of Alberta
Davit A. Potoyan: Iowa State University
Timothy E. Audas: Simon Fraser University

Nature Communications, 2024, vol. 15, issue 1, 1-15

Abstract: Abstract To survive, cells must respond to changing environmental conditions. One way that eukaryotic cells react to harsh stimuli is by forming physiological, RNA-seeded subnuclear condensates, termed amyloid bodies (A-bodies). The molecular constituents of A-bodies induced by different stressors vary significantly, suggesting this pathway can tailor the cellular response by selectively aggregating a subset of proteins under a given condition. Here, we identify critical structural elements that regulate heat shock-specific amyloid aggregation. Our data demonstrates that manipulating structural pockets in constituent proteins can either induce or restrict their A-body targeting at elevated temperatures. We propose a model where selective aggregation within A-bodies is mediated by the thermal stability of a protein, with temperature-sensitive structural regions acting as an intrinsic form of post-translational regulation. This system would provide cells with a rapid and stress-specific response mechanism, to tightly control physiological amyloid aggregation or other cellular stress response pathways.

Date: 2024
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DOI: 10.1038/s41467-024-45536-0

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