Tunneling nanotubes: A possible highway in the spreading of tau and other prion-like proteins in neurodegenerative diseases
Abstract
The mechanisms of intercellular spreading of amyloidogenic proteins involved inneurodegenerative diseases have yet to be fully elucidated. While secretion has been implicated inthe transfer of many proteins, including prions anda-synuclein, tunneling nanotubes (TNTs) havealso been demonstrated for prions and mutant Huntingtin. Here, we provide further evidence that Tauaggregates, which have been demonstrated to predominantly be transferred via secretion, can also befound in TNTs. Additionally, cells that have taken up Tau have increased TNT formation. Coupledwith previous evidence that other amyloidogenic aggregates also induce TNT formation we proposethat misfolded protein aggregates can, through a common mechanism, promote the formation ofTNTs and thereby their own intercellular transfer, contributing to the propagation of pathology