How the historically misunderstood amyloid helps to store memories

Newswise — KANSAS CITY, MO—For the first time, scientists from the Stowers Institute for Medical Research and collaborators have described the structure of an endogenously sourced, functioning neuronal amyloid at atomic resolution. The amyloid is composed of self-aggregated Orb2, the fruit fly version of the mRNA-binding cytoplasmic polyadenylation element-binding (CPEB) protein, which has been linked to long-term memory storage. The results of this work, published online March 13, 2020, in Science, have some very interesting implications.

“We thought the usual way amyloids arise is when a protein, having for some reason gone bad or become misfolded, cues amyloid formation in a stochastic, unregulated process,” explains Kausik Si, PhD, Stowers investigator and associate scientific director. “We found instead that amyloids can form at a very specific time, in a…

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