Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1934040 | Biochemical and Biophysical Research Communications | 2009 | 5 Pages |
Abstract
Interaction of the shortest isoform of tau protein (Ï3) 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 Ï3) strongly enhanced interaction of Ï3 with 14-3-3. Apparent KD of the complexes formed by phosphorylated Ï3 and 14-3-3 was close to 2 μM, whereas the corresponding constant for unphosphorylated Ï3 was at least 10 times higher. The stoichiometry of the complexes formed by phosphorylated Ï3 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 Ï3 and at the same time induced formation of crosslinked heterooligomeric complexes of Ï3 and 14-3-3 with an apparent molecular mass of 120-140 kDa.
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Authors
Nikolai N. Sluchanko, Alim S. Seit-Nebi, Nikolai B. Gusev,