Tau condensation on DNA mediates microtubule attachment suggesting a mitotic role for centromere-localized tau.

ABSTRACT: Tau protein, traditionally recognized for stabilizing microtubules and forming pathological aggregates, has recently been observed to form condensates in various contexts. While its condensation with RNA has been well studied, the interaction between tau and DNA, along with its biological significance, remains less explored. Here, using single-molecule experiments, we find that tau binds stably to naked DNA at nanomolar concentrations, leading to the local co-condensation of tau and DNA. These tau condensates on DNA can also interface with microtubules, leveraging tau's known role in promoting microtubule growth and organization. The dynamic nature of these condensates facilitates the remodeling of the DNA-microtubule assembly. Interestingly, phosphorylated tau and nucleosomal DNA exhibit

SUBMITTER: Park C 

PROVIDER: S-EPMC12855940 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature