Neuroscientists at the University of Iowa have identified a novel protein folding mechanism in the endoplasmic reticulum, which is essential for long-term memory storage.
The study shows that this mechanism is damaged in a tau-based mouse model of Alzheimer’s disease but if the protein folding mechanism is restored, it reverses the mouse model’s memory impairment for the study of dementia.
The findings of the study were published in March in the journal Science Advances.
Snehajyoti Chatterjee, director of the US-based Iowa Neuroscience Institute and associate in the laboratory of neuroscientist Ted Abel, led the team of researchers.
The team also used gene therapy to reactivate chaperone proteins in the mouse model and found that memory deficits were reversed. The team confirmed that the protein folding machinery works as a molecular switch for memory.
According to Chatterjee, the role of the protein folding machinery in long-term memory power has been ignored for decades.
“We know that gene expression and protein synthesis are essential for storing long-term memories. For proteins to be functionally active, they must be folded correctly. Our work demonstrates the concept that these chaperone proteins are those that fold or fold proteins to influence synaptic function and plasticity,” said Chatterjee.
Meanwhile, speaking about the research Ted Abel said, “Identifying this protein folding mechanism is an important step towards understanding how memories are stored and what goes wrong in diseases associated with memory loss, even though we are not at the point of taking care of a patient with this yet, understanding this pathway is essential to be able to one day prevent and treat neurodegenerative disease.”
