The shape of water at a key tau hotspot helps drive dementia-linked clumping
Researchers have identified a specific 'hotspot' on tau proteins that facilitates the misfolding and clumping associated with neurodegenerative diseases like Alzheimer's. This discovery offers a potential target for future therapeutic interventions to prevent the progression of tauopathies.
Why it matters
Understanding the molecular mechanism of protein misfolding is a critical step toward developing treatments for currently incurable neurodegenerative conditions.
edited by Swati Mestri , reviewed by Robert Egan
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Add to Preferred Sources Credit: Unsplash/CC0 Public Domain Diseases such as Alzheimer's and frontotemporal dementia are considered neurodegenerative tauopathies, in which tau proteins in the brain misfold and lead to cognitive decline. Until now, it has been unclear how misfolded tau recruits other seemingly healthy tau and causes it to misfold and clump.
A new study led by Northwestern University researchers, in collaboration with researchers at the University of California, Santa Barbara, found that tau vulnerable to misfolding carries a single dominant hotspot. That site binds to the matching site on a neighboring tau or on a tau at the end of an existing fibril, and the incoming tau then misfolds to match.
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