Effect of phosphorylation on interaction of human tau protein with 14-3-3ζ

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• 作者：Nikolai N. Sluchanko ; Alim S. Seit-Nebi ; Nikolai B. Gusev
• 关键词：14-3-3 ; Tau protein ; Phosphorylation ; Neurofibrillary tangles ; Alzheimer’ ; s disease
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2009
• 出版时间：20 February 2009
• 年：2009
• 卷：379
• 期：4
• 页码：990-994
• 全文大小：366 K

文摘

Interaction of the shortest isoform of tau protein (τ3) with human 14-3-3ζ was analyzed by means of native gel electrophoresis, chemical crosslinking and size-exclusion chromatography. Phosphorylation by cAMP-dependent protein kinase (up to 2 mole of phosphate per mole of τ3) strongly enhanced interaction of τ3 with 14-3-3. Apparent K_D of the complexes formed by phosphorylated τ3 and 14-3-3 was close to 2 μM, whereas the corresponding constant for unphosphorylated τ3 was at least 10 times higher. The stoichiometry of the complexes formed by phosphorylated τ3 and 14-3-3 was variable and was different from 1:1. 14-3-3 decreased the probability of formation of chemically crosslinked large homooligomers of phosphorylated τ3 and at the same time induced formation of crosslinked heterooligomeric complexes of τ3 and 14-3-3 with an apparent molecular mass of 120–140 kDa.