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DOI 10.1016/j.bbrc.2006.07.099
Title The self-assembly ability of First microtubule-binding repeat from tau and its modulation by phosphorylation
Creator/Author Zhou Lianxiu [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Zeng Zhiyang [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Du Jintang [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Zhao Yufen [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Li Yanmei [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)]. E-mail: liym@mail.tsinghua.edu.cn
Publication Date2006 Sep 22
OSTI IdentifierOSTI ID: 20854476
Other Number(s)Journal ID: ISSN 0006-291X; BBRCA9; TRN: US07R0251027466
Resource TypeJournal Article
Resource RelationJournal: Biochemical and Biophysical Research Communications; Journal Volume: 348; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2006.07.099; PII: S0006-291X(06)01660-3; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Subject60 APPLIED LIFE SCIENCES; DICHROISM; ELECTRON MICROSCOPY; FILAMENTS; MICROTUBULES; MODULATION; NERVOUS SYSTEM DISEASES; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; PHOSPHORYLATION; SPECTROSCOPY; TOXICITY
Description/Abstract Aggregation of abnormally phosphorylated tau in the form of tangs of paired helical filaments (PHFs) is one of the hallmarks of Alzheimer's disease (AD) and other tauopathies. It is of fundamental importance to study the mechanism of PHF formation and its modulation by phosphorylation. In this work, we have focused on First microtubule-binding repeat of tau encompassing an abnormal phosphorylation site Ser{sup 262}. The assembly propensities of this repeat and its corresponding phosphorylated form were investigated by turbidity and electron microscopy. Additionally, conformation of the two peptides is also analyzed through circular dichroism (CD) and NMR spectroscopy. Our results reveal that both of them are capable of self-assembly and phosphorylation at Ser{sup 262} could speed up the process of assembly. A possible mechanism of PHF formation is proposed and enhancing effect of phosphorylation on assembly provides an explanation to its toxicity in Alzheimer's disease.
Country of PublicationUnited States
LanguageEnglish
FormatSize: page(s) 637-642
System Entry Date2007 Apr 23

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