Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.

@article{Shen2003SignificanceO1,
  title={Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.},
  author={Ying Shen and Jakub Godlewski and Agnieszka Bronisz and Jun Zhu and Michael Comb and Joseph Avruch and Guri Tzivion},
  journal={Molecular biology of the cell},
  year={2003},
  volume={14 11},
  pages={
          4721-33
        }
}
14-3-3 proteins via binding serine/threonine-phosphorylated proteins regulate diverse intracellular processes in all eukaryotic organisms. Here, we examine the role of 14-3-3 self-dimerization in target binding, and in the susceptibility of 14-3-3 to undergo phosphorylation. Using a phospho-specific antibody developed against a degenerated mode-1 14-3-3 binding motif (RSxpSxP), we demonstrate that most of the 14-3-3-associated proteins in COS-7 cells are phosphorylated on sites that react with… CONTINUE READING