Intermolecular interactions and structure of R5L tau

Abstract

Tau is a multifunctional protein, most known for its role in the formation and stabilization of microtubules. Its six naturally occurring isoforms differ in the presence or absence of repeat regions in the N-terminus projection domain and C-terminal microtubule-binding region. Irregular tau polymerization correlates highly with the extent and localization of neurodegeneration in frontotemporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17). Mutations in the gene encoding tau have been shown to alter affinity for microtubules as well as kinetics, extent, and morphology of tau aggregation, and the extent of these differences depend on the tau isoform.