PubMed: 8391280

Title
Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments.
Journal
Neuron
Volume
10
Issue
None
Pages
1151-60
Date
1993-06-01
Authors
Takio K | Ihara Y | Morishima-Kawashima M | Titani K | Hasegawa M | Suzuki M

Evidence 3f8e5e9dac

Tau and dynactin show extensive colocalization, and the attachment of the dynactin complex to microtubules is enhanced by tau.

Evidence e5a976806c

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.

Evidence a09c29b77d

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.

Evidence ffa3d24855

The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region.

Evidence 9a8373afda

Ubiquitination occurs at lysines (K254, K257 K311) in repeat domain; participates in triage process

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