Divergent CPEB prion-like domains reveal different assembly mechanisms for a generic amyloid-like fold.

ABSTRACT:

Background

Amyloids are ordered, insoluble protein aggregates, characterized by a cross-β sheet quaternary structure in which molecules in a β-strand conformation are stacked along the filament axis via intermolecular interactions. While amyloids are typically associated with pathological conditions, functional amyloids have also been identified and are present in a wide variety of organisms ranging from bacteria to humans. The cytoplasmic polyadenylation element-binding (CPEB) prion-like protein is an mRNA-binding translation regulator, whose neuronal isoforms undergo activity-dependent aggregation, a process that has emerged as a plausible biochemical substrate for memory maintenance. CPEB aggregation is driven by prion-like domains (PLD) that are divergent in sequence across spe

SUBMITTER: Hervas R 

PROVIDER: S-EPMC7953810 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature