Tags

Type your tag names separated by a space and hit enter

O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau.
Biochem Biophys Res Commun. 2008 Oct 10; 375(1):59-62.BB

Abstract

In Alzheimer's disease (AD), tau protein is abnormally hyperphosphorylated and aggregated into paired helical filaments (PHFs). It was discovered recently that tau is also O-GlcNAcylated in human brains. And O-GlcNAcylation may regulate phosphorylation of tau in a site-specific manner. In this work, we focused on the fourth microtubule-binding repeat (R4) of tau, which has an O-GlcNAcylation site-Ser356. The aggregation behavior of this repeat and its O-GlcNAcylated form was investigated by turbidity, precipitation assay and electron microscopy. In addition, conformations of these two peptides were analyzed with circular dichroism (CD). Our results revealed that O-GlcNAcylation at Ser356 could greatly slow down the aggregation speed of R4 peptide. This modulation of O-GlcNAcylation on tau aggregation implies a new perspective of tau pathology.

Links

Publisher Full Text

Authors+Show Affiliations

Yu CH
Department of Chemistry, Beihua University, Jilin 132013, PR China.
Si T
No affiliation info available
Wu WH
No affiliation info available
Hu J
No affiliation info available
Du JT
No affiliation info available
Zhao YF
No affiliation info available
Li YM
No affiliation info available

MeSH

AcetylglucosamineAcylationAlzheimer DiseaseAmino Acid SequenceHumansMicrotubulesMolecular Sequence DataPeptidesProtein ConformationRepetitive Sequences, Amino AcidSerinetau Proteins

Pub Type(s)

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

Language

eng

PubMed ID

18671940

Citation

Yu, Chun-Hui, et al. "O-GlcNAcylation Modulates the Self-aggregation Ability of the Fourth Microtubule-binding Repeat of Tau." Biochemical and Biophysical Research Communications, vol. 375, no. 1, 2008, pp. 59-62.
Yu CH, Si T, Wu WH, et al. O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau. Biochem Biophys Res Commun. 2008;375(1):59-62.
Yu, C. H., Si, T., Wu, W. H., Hu, J., Du, J. T., Zhao, Y. F., & Li, Y. M. (2008). O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau. Biochemical and Biophysical Research Communications, 375(1), 59-62. https://doi.org/10.1016/j.bbrc.2008.07.101
Yu CH, et al. O-GlcNAcylation Modulates the Self-aggregation Ability of the Fourth Microtubule-binding Repeat of Tau. Biochem Biophys Res Commun. 2008 Oct 10;375(1):59-62. PubMed PMID: 18671940.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau. AU - Yu,Chun-Hui, AU - Si,Tong, AU - Wu,Wei-Hui, AU - Hu,Jia, AU - Du,Jin-Tang, AU - Zhao,Yu-Fen, AU - Li,Yan-Mei, Y1 - 2008/07/29/ PY - 2008/07/21/received PY - 2008/07/22/accepted PY - 2008/8/2/pubmed PY - 2008/9/10/medline PY - 2008/8/2/entrez SP - 59 EP - 62 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 375 IS - 1 N2 - In Alzheimer's disease (AD), tau protein is abnormally hyperphosphorylated and aggregated into paired helical filaments (PHFs). It was discovered recently that tau is also O-GlcNAcylated in human brains. And O-GlcNAcylation may regulate phosphorylation of tau in a site-specific manner. In this work, we focused on the fourth microtubule-binding repeat (R4) of tau, which has an O-GlcNAcylation site-Ser356. The aggregation behavior of this repeat and its O-GlcNAcylated form was investigated by turbidity, precipitation assay and electron microscopy. In addition, conformations of these two peptides were analyzed with circular dichroism (CD). Our results revealed that O-GlcNAcylation at Ser356 could greatly slow down the aggregation speed of R4 peptide. This modulation of O-GlcNAcylation on tau aggregation implies a new perspective of tau pathology. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/18671940/O_GlcNAcylation_modulates_the_self_aggregation_ability_of_the_fourth_microtubule_binding_repeat_of_tau_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(08)01450-2 DB - PRIME DP - Unbound Medicine ER -