14-3-3 Protein mediates phosphorylation of microtubule-associated protein tau by serum- and glucocorticoid-induced protein kinase 1.

The microtubule-associated protein, tau, is involved in numerous neuronal processes such as vesicle transport, microtubule-plasma membrane interaction and the intracellular localization of proteins. Tau is known to be phosphorylated by several kinases such as mitogen activated protein kinase, microtubule affinity regulating kinase, and protein kinase A. We found a putative ...
serum- and glucocorticoid-induced protein kinase 1 (SGK1) phosphorylation site within the 207GSRSRTPSLP216 tau amino acid sequence. We report here that SGK1 phosphorylates Ser214 of Tau. Using a pull-down assay, we found that 14-3-3q interacts with SGK1 and tau to form a ternary protein complex that leads to phosphorylation of tau. 14-3-3 and phosphorylated tau were mainly co-localized in the nucleus of COS-1 cells. These results demonstrate that 14-3-3 scaffolds tau with SGK1 to facilitate the phosphorylation of tau at Ser214 and to regulate its subcellular localization.
Mesh Terms:
14-3-3 Proteins, Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, COS Cells, Cell Line, Cell Nucleus, Cyclic AMP-Dependent Protein Kinases, Dose-Response Relationship, Drug, Humans, Immediate-Early Proteins, Immunoprecipitation, Microscopy, Fluorescence, Microtubules, Molecular Sequence Data, Mutagenesis, Site-Directed, Nuclear Proteins, Peptides, Phosphorylation, Protein Binding, Protein Isoforms, Protein-Serine-Threonine Kinases, Recombinant Proteins, Serine, Transfection, tau Proteins
Mol. Cells
Date: Dec. 31, 2004
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