Dynamic interactions and Ca²⁺-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding.

ABSTRACT: The microtubule-associated protein tau is implicated in the formation of oligomers and fibrillar aggregates that evade proteostasis control and spread from cell-to-cell. Tau pathology is accompanied by sustained neuroinflammation and, while the release of alarmin mediators aggravates disease at late stages, early inflammatory responses encompass protective functions. This is the case of the Ca²⁺-binding S100B protein, an astrocytic alarmin which is augmented in AD and which has been recently implicated as a proteostasis regulator, acting over amyloid β aggregation. Here we report the activity of S100B as a suppressor of tau aggregation and seeding, operating at sub-stoichiometric conditions. We show that S100B interacts with tau in living cells even in microtubule-destabilizing

SUBMITTER: Moreira GG 

PROVIDER: S-EPMC8560819 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature