Abstract
Intra- and extra-cellular amyloid protein fibers are traditionally coupled to a series of devastating and incurable neurodegenerative disorders. Since the discovery of physiologically useful amyloids, our attention has been shifting from pure pathology to function, as amyloid aggregation seems to constitute a basis for the functional and dynamic assembly of biological structures. The following article summarizes how the cell profits from such an unconventional high-risk aggregation at the rim of physiologic utility and pathologic catastrophe.