Polymerization of [tau] into Filaments in the Presence of Heparin: The Minimal Sequence Required for [tau] - [tau] Interaction.
Perez, Mar; Valpuesta, Jose M. *; Medina, Miguel; Montejo de Garcini, Esteban; Avila, Jesus
[Miscellaneous Article] Journal of Neurochemistry. 67(3):1183-1190, September 1996.

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Paired helical filaments isolated from the brains of patients with Alzheimer's disease are composed of a major protein component, the microtubule-associated protein termed [tau], together with other nonprotein components, including heparan, a glycosaminoglycan, the more extensively sulfated form of which is heparin. As some of these nonprotein components may modulate the assembly of [tau] into filamentous structures, we have analyzed the ability of the whole [tau] protein or some of its fragments to self-assemble in the presence of heparin. Different [tau] fragments, all of them containing some sequences of the tubulin-binding motif, can assemble in vitro into filaments. We have also found formation of polymers with the 18-residue-long peptide corresponding to the third tubulin-binding motif of [tau]. This suggests that the ability of [tau] for self-assembly could be localized in a short sequence of amino acids present in the tubulin-binding repeats of the [tau] molecule.

(C) 1996 International Society for Neurochemistry