Abstract
Historically, amyloids were perceived as toxic/irreversible protein aggregates associated with neurodegenerative disorders including Alzheimer’s and Parkinson’s diseases. Recent papers are challenging this perception by uncovering widespread cellular roles for physiological amyloidogenesis. These findings suggest that the amyloid-fold should be considered, alongside the native-fold and unfolded configurations, as a physiological and reversible protein organization.
Cells exploit the amyloid fibrillation propensity of proteins in physiology.
Systemic physiological amyloidogenesis programs induce a state of dormancy.
Amyloid-like assemblies exhibit properties of solid-state protein organization.
Insights from physiological amyloidogenesis open potential novel avenues of investigation for amyloid pathogenesis.
