Altered tubulin assembly dynamics with N-homocysteinylated human 4R/1N tau in vitro

► We modified tau by N-homocysteinylation (0.15, 1.5 and 15mM). ► We found that 25 Lys residues are particularly susceptible to modification in the presence of 15mM tHcy. ► Binding of tau to MTP is inhibited upon modification, depending on the degree of N-homocysteinylation. ► N-Hcy-tau species, com...

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Veröffentlicht in:	FEBS letters 2012-11, Vol.586 (21), p.3914-3919
Hauptverfasser:	Karima, Oveis, Riazi, Gholamhossein, Khodadadi, Sirus, Aryapour, Hassan, Nasiri Khalili, Mohammad Ali, Yousefi, Leila, Moosavi-Movahedi, Ali Akbar
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Brain - metabolism Cattle Homocysteine - chemistry Homocysteine - metabolism Homocysteine thiolactone Humans Microtubule protein Microtubules - chemistry Microtubules - metabolism N-Homocysteinylation Phosphorylation Protein Binding Protein Isoforms - chemistry Protein Isoforms - metabolism Solutions Tau protein (4R/1N) tau Proteins - chemistry tau Proteins - metabolism Tubulin - chemistry Tubulin - metabolism
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