Differential binding affinity of tau repeat region R2 with neuronal-specific β-tubulin isotypes.

ABSTRACT: Tau is a microtubule-associated protein whose C-terminal domain consisting of four repeat regions R1, R2, R3 and R4 binds to microtubules to stabilize them. In several neurodegenerative diseases, tau detaches from microtubules to form insoluble aggregates leading to tauopathy. Microtubules are made up of αβ tubulin subunits. Seven α-tubulin and nine β-tubulin isotypes have been reported to be present in humans till date. These tubulin isotypes show residue composition variations mainly at C-terminal region and bind to motor proteins and anti-mitotic drugs differently. These tubulin isotypes show tissue specific expression as their relative proportion varies significantly in different type of cells. It is also known that tau binds differently to different cell lines and can either promote o

SUBMITTER: Bhandare VV 

PROVIDER: S-EPMC6658543 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature