Tau and dynactin show extensive colocalization, and the attachment of the dynactin complex to microtubules is enhanced by tau.
Mutations of a conserved arginine residue in the Nterminus of tau, found in patients with FTDP-17, affect its binding to dynactin, which is abnormally distributed in the retinal ganglion cell axons of transgenic mice expressing human tau with a mutation in the microtubule-binding domain.
We show here for the first time that the N-terminal projection domain of tau binds to the C-terminus of the p150 subunit of the dynactin complex. The sequences of tau encoded by exons 1 and 4, which lie at the tip of the N-terminal projection domain, interact with the C-terminal region of p150.
The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region.
Ubiquitination occurs at lysines (K254, K257 K311) in repeat domain; participates in triage process
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.