Disulfide bond formation in microtubule-associated tau protein promotes tau accumulation and toxicity in vivo.

ABSTRACT: Accumulation of microtubule-associated tau protein is thought to cause neuron loss in a group of neurodegenerative diseases called tauopathies. In diseased brains, tau molecules adopt pathological structures that propagate into insoluble forms with disease-specific patterns. Several types of posttranslational modifications in tau are known to modulate its aggregation propensity in vitro, but their influence on tau accumulation and toxicity at the whole-organism level has not been fully elucidated. Herein, we utilized a series of transgenic Drosophila models to compare systematically the toxicity induced by five tau constructs with mutations or deletions associated with aggregation, including substitutions at seven disease-associated phosphorylation sites (S7A and S7E), deletions of PHF6 an

SUBMITTER: Saito T 

PROVIDER: S-EPMC8522637 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature