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Altered tubulin assembly dynamics with N ‐homocysteinylated human 4R/1N tau in vitro
Author(s) -
Karima Oveis,
Riazi Gholamhossein,
Khodadadi Sirus,
Aryapour Hassan,
Nasiri Khalili Mohammad Ali,
Yousefi Leila,
Moosavi-Movahedi Ali Akbar
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.09.024
Subject(s) - gene isoform , microtubule , hyperphosphorylation , tubulin , tau protein , in vitro , microbiology and biotechnology , chemistry , lysine , plasma protein binding , biochemistry , function (biology) , biology , alzheimer's disease , phosphorylation , disease , amino acid , medicine , gene
Tau isoforms promote neuronal integrity through binding and stabilization of microtubule proteins (MTP). It has been shown that hyperphosphorylation of tau contributes to Alzheimer's disease (AD) pathology and related tauopathies. However, other pathogenic modifications of tau have not been well characterized. It is well accepted that elevated level of homocysteine (Hcy) is associated with neurodegenerative diseases such as AD. As a result of N ‐homocysteinylation of lysine residues, Hcy becomes a component of proteins, as a protein–homocystamide adduct, which affects protein structure and function. Here we demonstrate that N ‐homocysteinylation of human tau (4R/1N isoform) inhibits its function via impaired tau–tubulin specific binding and MTP assembly dynamics in vitro.