Quinones Facilitate the Self-Assembly of the Phosphorylated Tubulin Binding Region of Tau into Fibrillar Polymers.

The fragment of tau containing the first and third tubulin-binding motifs, involved in self- assembly of tau, was phosphorylated by protein kinase A (PKA). In the presence of hydroxynonenal (HNE) or in the presence of quinones such as juglone, 2,3-dimethoxy-5-methyl-1,4-benzoquinone (coenzyme Q0 or...

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Detalles Bibliográficos
Autores: Santa-María, Ismael, Hernandez, Felix, Perez Martın, Concepción, Avila, Jesús, Moreno, Francisco J.
Tipo de recurso: artículo
Fecha de publicación:2004
País:España
Institución:Universidad Francisco de Vitoria
Repositorio:DDFV. Repositorio Institucional de la Universidad Francisco de Vitoria
Idioma:inglés
OAI Identifier:oai:ddfv.ufv.es:10641/3624
Acceso en línea:https://hdl.handle.net/10641/3624
Access Level:acceso abierto
Descripción
Sumario:The fragment of tau containing the first and third tubulin-binding motifs, involved in self- assembly of tau, was phosphorylated by protein kinase A (PKA). In the presence of hydroxynonenal (HNE) or in the presence of quinones such as juglone, 2,3-dimethoxy-5-methyl-1,4-benzoquinone (coenzyme Q0 or DMM), or menadione, the polymerization of this phosphorylated tau fragment is catalyzed, whereas polymerization of the unmodified fragment takes place in a lesser extent. The quinones coenzyme Q0 and menadione are found in every cell, including neural cells, and may interact with tau protein to facilitate its assembly into filamentous structures. These tau filaments, assembled in the presence of quinones, have a fibrillar morphology very similar to that of paired helical filaments present in the brains of patients with Alzheimer’s disease.