The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface.

@article{Woodcock2003TheDV,
  title={The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface.},
  author={Joanna M Woodcock and Jane Murphy and Frank C. Stomski and Michael C. Berndt and Angel F Lopez},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 38},
  pages={36323-7}
}
The 14-3-3 proteins play a central role in the regulation of cell growth, cycling, and apoptosis by modulating the functional activities of key signaling proteins. Through binding to a phosphoserine motif, 14-3-3 alters target proteins activities by sequestering them, relocalizing them, conformationally altering their functional activity, or by promoting interaction with other proteins. These functions of 14-3-3 are facilitated by, if not dependent on, its dimeric structure. We now show that… CONTINUE READING