Tau antagonizes end-binding protein tracking at microtubule ends through a phosphorylation-dependent mechanism.

ABSTRACT: Proper regulation of microtubule dynamics is essential for cell functions and involves various microtubule-associated proteins (MAPs). Among them, end-binding proteins (EBs) accumulate at microtubule plus ends, whereas structural MAPs bind along the microtubule lattice. Recent data indicate that the structural MAP tau modulates EB subcellular localization in neurons. However, the molecular determinants of EB/tau interaction remain unknown, as is the effect of this interplay on microtubule dynamics. Here we investigate the mechanisms governing EB/tau interaction in cell-free systems and cellular models. We find that tau inhibits EB tracking at microtubule ends. Tau and EBs form a complex via the C-terminal region of EBs and the microtubule-binding sites of tau. These two domains are require

SUBMITTER: Ramirez-Rios S 

PROVIDER: S-EPMC5042579 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature