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

详细信息    查看全文

• 作者：Ismael Santa-Marí ; a ; Fé ; lix Herná ; ndez ; Concepci&oacute ; n Pé ; rez Martí ; n ; Jesú ; s Avila ; and Francisco J. Moreno
• 刊名：Biochemistry
• 出版年：2004
• 出版时间：March 16, 2004
• 年：2004
• 卷：43
• 期：10
• 页码：2888 - 2897
• 全文大小：414K
• 年卷期：v.43,no.10(March 16, 2004)
• ISSN：1520-4995

文摘

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 coenzymeQ₀ and menadione are found in every cell, including neural cells, and may interact with tau protein tofacilitate its assembly into filamentous structures. These tau filaments, assembled in the presence ofquinones, have a fibrillar morphology very similar to that of paired helical filaments present in the brainsof patients with Alzheimer's disease.