Overview:

14-3-3beta is a member of the highly conserved family of 14-3-3 proteins that appear to have multiple roles in cell signaling by binding to phosphoserine-containing proteins (1). 14-3-3 proteins are abundantly expressed in the brain and have been detected in the cerebrospinal fluid of patients with different types of neurological disorders (2). 14-3-3 proteins bind and regulate protein ligands that are typically phosphorylated on serine or threonine residues (3). 14-3-3 proteins affect a diverse array of cellular processes including the cell cycle and transcription, signal transduction and intracellular trafficking. 14-3-3 proteins function as a dimer. Dimerization of the 14-3-3 protein is regulated by site-specific serine phosphorylation (4).

References:

1. Yaffe, M B. et al: The structure basis for 14-3-3:phosphopeptide binding specificity. Cell 1997 91: 961-971.

2. Berg, D. et al.: 14-3-3 Proteins in the nervous system. Nat Rev Neurosci 2003 4:752-762.

3. Silhan, J. et al.: 14-3-3 Protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding. J Biol Chem 2004 279:49113-49119.

4. Woodcock, J M. et al: The dimeric versus monomeric status of 14-3-3 zeta is controlled by phosphorylation of Ser58 at the dimer interface. J Biol Chem 2003 278:36323-36327.