Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats.

ABSTRACT: Tau is a microtubule-associated protein that is genetically linked to dementia and linked to Alzheimer's disease via its presence in intraneuronal neurofibrillary tangle deposits, where it takes the form of aggregated paired helical and straight filaments. Although the precise mechanisms by which tau contributes to neurodegeneration remain unclear, tau aggregation is commonly considered to be a critical component of tau-mediated pathogenicity. Nevertheless, the context in which tau aggregation begins in vivo is unknown. Tau is enriched in membrane-rich neuronal structures such as axons and growth cones, and can interact with membranes both via intermediary proteins and directly via its microtubule-binding domain (MBD). Membranes efficiently facilitate tau aggregation in vitro, and may ther

SUBMITTER: Georgieva ER 

PROVIDER: S-EPMC4167292 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature