KANSAS CITY, MO — January 26, 2026 — In a breakthrough that could reshape our understanding of memory, researchers at the Stowers Institute have identified a mechanism that turns fleeting moments into lasting memories. This discovery, the result of over two decades of research, reveals that the nervous system can deliberately form amyloids to convert sensory experiences into enduring memories. The findings challenge long-held beliefs about memory and amyloid formation in the brain, offering new potential treatments for amyloid-related neurological disorders.
“I wanted to understand how unstable proteins help create stable memories,” said Dr. Kausik Si, Scientific Director at the Stowers Institute. “Now, we have definitive evidence that there are processes within the nervous system that can take a protein and make it form an amyloid at a very specific time, in a specific place, and in response to a specific experience.”
Amyloids: From Disease-Associated to Memory-Forming
Published in the Proceedings of the National Academy of Sciences on January 30, 2026, the study focuses on “chaperone proteins” in fruit flies. Traditionally, chaperones are known to assist in protein folding, preventing harmful misfolding. However, the researchers identified a specific chaperone that allows proteins to change shape and form functional amyloids, essential for long-term memory storage.
“This expands the idea of a protein’s capacity to do meaningful things and suggests there is an unknown universe of chaperone biology that we’ve long been missing,” Si explained.
Amyloids are often linked to neurodegenerative diseases like Alzheimer’s and Parkinson’s, where they form stable, destructive protein fibers. However, the new research supports the Si Lab’s 2020 study, which proposed that amyloids can also be beneficial, serving as tools for memory storage when properly regulated.
Unraveling the Chaperone’s Role
The pivotal discovery of a functional amyloid in a sea slug in 2003 laid the groundwork for this research. With just 10,000 neurons, the sea slug provided a simplified model for studying amyloid biology. The research then expanded to more complex organisms, including fruit flies, mice, and humans, revealing that amyloid-based mechanisms are broadly used for memory persistence.
In fruit flies, a prion-like protein called Orb2 must self-assemble at synapses to maintain a memory. The researchers hypothesized that the difference between harmful and helpful amyloids might depend on whether Orb2’s assembly is tightly regulated by other proteins. This study allowed them to test that hypothesis, leading to the discovery of a previously uncharacterized chaperone named Funes.
“We were inspired by Jorge Luis Borges’ short story Funes the Memorious, in which one man’s perfect memory comes at a cost, so we named the chaperone Funes,” said Dr. Kyle Patton, lead author of the study.
Implications for Memory and Disease
The researchers discovered Funes by manipulating concentrations of 30 different chaperones in the fly’s memory centers. Flies with increased Funes levels showed remarkable long-term memory retention, linking a specific smell with a sugar reward. At a molecular level, Funes variants that could bind Orb2 but not trigger amyloid transition led to memory failure, underscoring Funes’ crucial role in memory formation.
“We are now getting early evidence that, like the fruit fly shows in this study, the process may also manifest in the vertebrate nervous system,” Si noted. “Our hypothesis is carrying us all the way to the vertebrate brain, illustrating that it may actually be universal.”
While screening chaperone proteins, the team found an unexpected connection to human health. “If you look at the human version of these genes, they have surprisingly been implicated in schizophrenia,” Patton said. This opens the possibility that chaperones could be key factors in neurological disorders, potentially acting as mediators.
“Ultimately, chaperones may allow the brain to perceive, process, or store information about the outside world,” Si said. “And in diseases where we do not see the world as it is, like schizophrenia or bipolar disorder, we could imagine chaperones playing a role.”
Looking Forward
This groundbreaking research not only enhances our understanding of memory formation but also suggests new therapeutic avenues for amyloid-related diseases. By activating specific chaperones, it may be possible to guide toxic amyloids to be less harmful or enhance the brain’s capacity to form functional amyloids, potentially overriding disease-causing amyloids.
The study was funded by the University of Hong Kong, the Research Grant Council of Hong Kong, and the Stowers Institute for Medical Research. Additional authors include Yangyang Yi, Ph.D., Raj Burt, Kevin K-S. Ng, Ph.D., Mayur Mukhi, and Peerzada Shariq Shaheen Khaki, Ph.D.
Founded in 1994, the Stowers Institute for Medical Research is a non-profit organization dedicated to foundational biomedical research. With over 370 scientific staff, the Institute aims to expand our understanding of life’s secrets and improve quality of life through innovative research.
