Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 2008 Oct 10;375(1):59-62. doi: 10.1016/j.bbrc.2008.07.101. Epub 2008 Jul 29.

O-GlcNAcylation modulates the self-aggregation ability of the fourth microtubule-binding repeat of tau.

Author information

1
Department of Chemistry, Beihua University, Jilin 132013, PR China.

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.

PMID:
18671940
DOI:
10.1016/j.bbrc.2008.07.101
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center