Reversible Cation-Selective Attachment and Self-Assembly of Human Tau on Supported Brain Lipid Membranes.

ABSTRACT: Misfolding and aggregation of the neuronal, microtubule-associated protein tau is involved in the pathogenesis of Alzheimer's disease and tauopathies. It has been proposed that neuronal membranes could play a role in tau release, internalization, and aggregation and that tau aggregates could exert toxicity via membrane permeabilization. Whether and how tau interacts with lipid membranes remains a matter of discussion. Here, we characterize the interaction of full-length human tau (htau40) with supported lipid membranes (SLMs) made from brain total lipid extract by time-lapse high-resolution atomic force microscopy (AFM). We observe that tau attaches to brain lipid membranes where it self-assembles in a cation-dependent manner. Sodium triggers the attachment, self-assembly, and growth, wher

SUBMITTER: Mari SA 

PROVIDER: S-EPMC6588182 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature