The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics.

ABSTRACT: The pathological accumulation of abnormally hyperphosphorylated and aggregated tau, a neuronal microtubule (MT)-associated protein that functions to maintain MT stability, is implicated in a number of hereditary and sporadic neurodegenerative diseases including frontotemporal dementia and Alzheimer's disease. Targeting tau for the treatment of these diseases is an area of intense interest and toward that end, modulation of cellular molecular chaperones is a potential therapeutic target. In particular, the constitutive Hsp70 isoform, Hsc70, seems highly interconnected with tau, preserving tau protein levels and synergizing with it to assemble MTs. But the relationship between tau and Hsc70, as well as the impact of this interaction in neurons and its therapeutic implications remain unknown.

SUBMITTER: Fontaine SN 

PROVIDER: S-EPMC4560066 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature