Parker Team Cuts Tau Clumps With FAF2, Improving Brain Function in 80% Disease Target
Updated
Updated · Newswise · Jun 27
Parker Team Cuts Tau Clumps With FAF2, Improving Brain Function in 80% Disease Target
1 articles · Updated · Newswise · Jun 27
Summary
Mouse models showed better brain function after Roy Parker’s team steered the quality-control protein FAF2 to tau aggregates, shrinking the toxic clumps and protecting neurons.
Real-time imaging traced how misfolded tau seeds enter cells, latch onto RNA-processing assemblies and recruit normal tau into larger aggregates that accelerate cellular damage.
SRRM2 emerged as a key partner in that process: its polyserine segment binds tightly to tau, and the team repurposed that interaction as an address tag to deliver FAF2 directly to the clumps.
Tau is implicated in about 80% of neurodegenerative diseases, and SRRM2 was also found alongside tau clumps in post-mortem Alzheimer’s tissue, suggesting the mechanism may operate in people.
Parker said the next step could be a drug that links FAF2 to tau aggregates, aiming for an accessible therapy as dementia is expected to affect nearly 50% of people as patients or caregivers.
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Overview
Roy Parker’s team at the University of Colorado has made a major breakthrough in understanding tau pathology, a key factor in many neurodegenerative diseases. Their research used advanced imaging to watch misfolded tau protein seeds as they entered cells and joined with RNA-binding proteins like SRRM2, which normally helps with RNA processing. This process leads to the formation of harmful tau clumps. Importantly, the team discovered that the protein FAF2 can disrupt these tau aggregates, offering a promising new approach for treating diseases where tau pathology is central. This innovative strategy could help many people affected by neurodegenerative conditions.