Phospho-Ser/Thr Binding: 14-3-3 Domain
Human 14-3-3 ζ dimer bound to TrkA phospho-peptide (red).
Domain Binding and Function
14-3-3 proteins are 30 kDa polypeptides with nine closely related members in mammals. They are also found in plants and fungi. They are involved in regulating various pathways including signaling apoptosis and passage through the cell cycle. 14-3-3 proteins form homo and heterodimeric cup-like structures that bind to discrete phosphoserine-containing motifs. In some instances, 14-3-3 proteins appear to export their binding partners from the nucleus to the cytoplasm in a phosphorylationand Crm1-dependent manner.
Structure Reference
- Rittinger, K. et al. (1999) Mol. Cell 4, 153.
Examples of Domain Proteins
Binding Examples
| 14-3-3 Binding Partners | Functions |
|---|---|
| cdc25 tyrosine phosphatase | Cell cycle regulation |
| Bad Bcl-xL binding partner | Regulation of apoptosis |
| c-Raf Ser/Thr Kinase | Regulation of kinase activity; Signal transduction |
| PKC Ser/Thr Kinase | Signal transduction |
| MEKK1,2,3 Ser/Thr Kinase | Signal transduction |
Consensus Binding Sites
R-X-[Ar/S]-[+]-pS-[LEAM]-P or R-[S/Ar]-[+]-pS-[LEAM]-P
Where Ar=aromatic residue, [+]=basic residue and pS=phosphoserine
