Tau-RNA complexes inhibit microtubule polymerization and drive disease-relevant conformation change.

ABSTRACT: Alzheimer's disease and related disorders feature neurofibrillary tangles and other neuropathological lesions composed of detergent-insoluble tau protein. In recent structural biology studies of tau proteinopathy, aggregated tau forms a distinct set of conformational variants specific to the different types of tauopathy disorders. However, the constituents driving the formation of distinct pathological tau conformations on pathway to tau-mediated neurodegeneration remain unknown. Previous work demonstrated RNA can serve as a driver of tau aggregation, and RNA associates with tau containing lesions, but tools for evaluating tau/RNA interactions remain limited. Here, we employed molecular interaction studies to measure the impact of tau/RNA binding on tau microtubule binding and aggregation.

SUBMITTER: McMillan PJ 

PROVIDER: S-EPMC10393409 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature