Abstract：
:The microtubule-associated protein Tau plays a central role in the pathogenesis of Alzheimer's disease. Although Tau interaction with membranes is thought to affect some of its physiological functions and its aggregation properties, the sequence determinants and the structural and functional consequences of such interactions remain poorly understood. Here, we report that the interaction of Tau with vesicles results in the formation of highly stable protein/phospholipid complexes. These complexes are toxic to primary hippocampal cultures and are detected by MC-1, an antibody recognizing pathological Tau conformations. The core of these complexes is comprised of the PHF6* and PHF6 hexapeptide motifs, the latter in a β-strand conformation. Studies using Tau-derived peptides enabled the design of mutants that disrupt Tau interactions with phospholipids without interfering with its ability to form fibrils, thus providing powerful tools for uncoupling these processes and investigating the role of membrane interactions in regulating Tau function, aggregation and toxicity.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Ait-Bouziad N,Lv G,Mahul-Mellier AL,Xiao S,Zorludemir G,Eliezer D,Walz T,Lashuel HAdoi
10.1038/s41467-017-01575-4subject
Has Abstractpub_date
2017-11-22 00:00:00pages
1678issue
1issn
2041-1723pii
10.1038/s41467-017-01575-4journal_volume
8pub_type
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