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The self-assembly ability of the first microtubule-binding repeat from tau and its modulation by phosphorylation.
Biochem Biophys Res Commun. 2006 Sep 22; 348(2):637-42.BB

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 the first microtubule-binding repeat of tau encompassing an abnormal phosphorylation site Ser262. 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 Ser262 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.

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Authors+Show Affiliations

Zhou LX
Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, PR China.
Zeng ZY
No affiliation info available
Du JT
No affiliation info available
Zhao YF
No affiliation info available
Li YM
No affiliation info available

MeSH

Amino Acid SequenceBinding SitesHumansMicroscopy, ElectronNuclear Magnetic Resonance, BiomolecularPeptide FragmentsPhosphopeptidesPhosphorylationProtein Structure, QuaternaryTubulintau Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16889747

Citation

Zhou, Lian-Xiu, et al. "The Self-assembly Ability of the First Microtubule-binding Repeat From Tau and Its Modulation By Phosphorylation." Biochemical and Biophysical Research Communications, vol. 348, no. 2, 2006, pp. 637-42.
Zhou LX, Zeng ZY, Du JT, et al. The self-assembly ability of the first microtubule-binding repeat from tau and its modulation by phosphorylation. Biochem Biophys Res Commun. 2006;348(2):637-42.
Zhou, L. X., Zeng, Z. Y., Du, J. T., Zhao, Y. F., & Li, Y. M. (2006). The self-assembly ability of the first microtubule-binding repeat from tau and its modulation by phosphorylation. Biochemical and Biophysical Research Communications, 348(2), 637-42.
Zhou LX, et al. The Self-assembly Ability of the First Microtubule-binding Repeat From Tau and Its Modulation By Phosphorylation. Biochem Biophys Res Commun. 2006 Sep 22;348(2):637-42. PubMed PMID: 16889747.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The self-assembly ability of the first microtubule-binding repeat from tau and its modulation by phosphorylation. AU - Zhou,Lian-Xiu, AU - Zeng,Zhi-Yang, AU - Du,Jin-Tang, AU - Zhao,Yu-Fen, AU - Li,Yan-Mei, Y1 - 2006/07/28/ PY - 2006/07/18/received PY - 2006/07/20/accepted PY - 2006/8/8/pubmed PY - 2006/10/13/medline PY - 2006/8/8/entrez SP - 637 EP - 42 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 348 IS - 2 N2 - 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 the first microtubule-binding repeat of tau encompassing an abnormal phosphorylation site Ser262. 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 Ser262 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. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/16889747/The_self_assembly_ability_of_the_first_microtubule_binding_repeat_from_tau_and_its_modulation_by_phosphorylation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(06)01660-3 DB - PRIME DP - Unbound Medicine ER -