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Updated: Jun 26, 2026

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
Published on: October 10, 2017
Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta
Nikolai N Sluchanko1, Alim S Seit-Nebi, Nikolai B Gusev
1Department of Biochemistry, School of Biology, M.V. Lomonosov Moscow State University, Moscow 119991, Russian Federation.
Abstract:
Interaction of the shortest isoform of tau protein (tau3) with human 14-3-3zeta 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 tau3) strongly enhanced interaction of tau3 with 14-3-3. Apparent K(D) of the complexes formed by phosphorylated tau3 and 14-3-3 was close to 2 microM, whereas the corresponding constant for unphosphorylated tau3 was at least 10 times higher. The stoichiometry of the complexes formed by phosphorylated tau3 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 tau3 and at the same time induced formation of crosslinked heterooligomeric complexes of tau3 and 14-3-3 with an apparent molecular mass of 120-140 kDa.
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