Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta.
Serine residues phosphorylated by protein kinase A (PKA) in the shortest isoform of human tau protein (tau3) were sequentially replaced by alanine and interaction of phosphorylated tau3 and its mutants with 14-3-3 was investigated. Mutation S156A slightly decreased interaction of phosphorylated tau3 with 14-3-3. Double mutations S156A/S267A and especially S156A/S235A, ... strongly inhibited interaction of phosphorylated tau3 with 14-3-3. Thus, two sites located in the Pro-rich region and in the pseudo repeats of tau3 are involved in phosphorylation-dependent interaction of tau3 with 14-3-3. The state of tau3 phosphorylation affects the mode of 14-3-3 binding and by this means might modify tau filament formation.
Mesh Terms:
14-3-3 Proteins, Cyclic AMP-Dependent Protein Kinases, Humans, Phosphorylation, Point Mutation, Protein Isoforms, Serine, tau Proteins
14-3-3 Proteins, Cyclic AMP-Dependent Protein Kinases, Humans, Phosphorylation, Point Mutation, Protein Isoforms, Serine, tau Proteins
FEBS Lett.
Date: Sep. 03, 2009
PubMed ID: 19647741
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