HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

ABSTRACT: The microtubule-associated protein tau forms insoluble, amyloid-type aggregates in various dementias, most notably Alzheimer's disease. Cellular chaperone proteins play important roles in maintaining protein solubility and preventing aggregation in the crowded cellular environment. Although tau is known to interact with numerous chaperones, it remains unclear how these chaperones function mechanistically to prevent tau aggregation and how chaperones from different classes compare in terms of mechanism. Here, we focused on the small heat shock protein HspB1 (also known as Hsp27) and the constitutive chaperone Hsc70 (also known as HspA8) and report how each chaperone interacts with tau to prevent its fibril formation. Using fluorescence and NMR spectroscopy, we show that the two chaperones i

SUBMITTER: Baughman HER 

PROVIDER: S-EPMC5827454 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature