Article

Title:Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta.
Authors:Sluchanko NN; Seit-Nebi AS; Gusev NB
Publication:FEBS Lett. 2009 Sep 3;583(17):2739-42. doi: 10.1016/j.febslet.2009.07.043. Epub 2009 Aug 3.
PubmedID19647741
Abstract
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.