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11 Dec 2020 As a person’s symptoms of Alzheimer’s disease emerge and worsen, tau tangles spread inexorably through the cortex. What unfortunate series of events pushes this microtubule-binding protein into a cataclysmic state? In a paper published November 10 in Cell, researchers led by Judith Steen at Boston Children’s Hospital addressed this question by mapping and quantifying myriad post-translational modifications of the tau protein extracted from more than 90 human brain samples. From truncation to phosphorylation, from acetylation to ubiquitination, the researchers identified modifications that distinguished people with AD from controls. They described an ordered piling-on of alterations that tracked with disease stage. Some of these same modifications adorn tau species that seed aggregation. Ubiquitination stood out as a potential culprit. In all, the findings could help researchers zero in on which species of tau to target therapeutically, and suggest different targets

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