Structures of filaments from Pick's disease reveal a novel tau protein fold.

ABSTRACT: The ordered assembly of tau protein into abnormal filamentous inclusions underlies many human neurodegenerative diseases¹. Tau assemblies seem to spread through specific neural networks in each disease², with short filaments having the greatest seeding activity³. The abundance of tau inclusions strongly correlates with disease symptoms⁴. Six tau isoforms are expressed in the normal adult human brain-three isoforms with four microtubule-binding repeats each (4R tau) and three isoforms that lack the second repeat (3R tau)¹. In various diseases, tau filaments can be composed of either 3R or 4R tau, or of both. Tau filaments have distinct cellular and neuroanatomical distributions⁵, with morphological and biochemical differences

SUBMITTER: Falcon B 

PROVIDER: S-EPMC6204212 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature