AD is typically characterized by intracellular tangles of tau and extracellular
amyloid-beta plaques. In the development of AD, amyloid-beta is thought to
induce tau phosphorylation, leading to dysfunction of neurons. The precise
mechanism of how amyloid-beta and tau work together to coordinate
dysfunction in neurons of AD patients remains unclear.
In contrast to the prevailing idea in the field, the authors of this study
presented a novel hypothesis: site-specific phosphorylation of tau inhibits
amyloid-beta toxicity, at least in the early stages of the disease. Using an AD
mouse model, these researchers examined the possibility of tau playing a
protective role in AD development.
Using MST, the authors complemented their in vitro binding data and confirmed
their novel hypothesis that site-specific phosphorylation of tau can inhibit
amyloid-beta toxicity in the early stages of AD.
Find a novel role for
phosphorylated tau on
amyloid-beta toxicity
4
Molecular
interactions
studied
Target: Tau
Ligand: PSD-95
Method used
MST using Monolith
Learn more
8
