Membrane interaction and disulphide-bridge formation in the unconventional secretion of Tau.

ABSTRACT: Misfolded, pathological tau protein propagates from cell to cell causing neuronal degeneration in Alzheimer's disease and other tauopathies. The molecular mechanisms of this process have remained elusive. Unconventional secretion of tau takes place via several different routes, including direct penetration through the plasma membrane. Here, we show that tau secretion requires membrane interaction via disulphide bridge formation. Mutating residues that reduce tau interaction with membranes or formation of disulphide bridges decrease both tau secretion from cells, and penetration through artificial lipid membranes. Our results demonstrate that tau is indeed able to penetrate protein-free membranes in a process independent of active cellular processes and that both membrane interaction and di

SUBMITTER: Hellen M 

PROVIDER: S-EPMC8350431 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature