Regulation of 14-3-3 proteins

Study of 14-3-3 acetylation during the cell cycle, differentiation and reprogramming. Lysine residue 49 (K49) is part of the phosphate group recognition site on 14-3-3 client phosphoproteins, and its modification (by acetylation) results in an inactive 14-3-3 protein. We are investigating the acetylation of 14-3-3 in this residue, its biological function, the upstream factors that trigger it and the relevant events in physiology and cellular processes that could be affected by the inactivation of 14-3-3. Thus, we study the mechanism by which a post-translational modification (acetylation) would globally affect another modification (phosphorylation).

14-3-3 β-carboline interactions.

The β carbolines are organic aromatic compounds that participate in various normal biological processes, and have also been related to pathologies induced by radiation, cancer and Parkinson's. By in silico methods we have found that a compound belonging to the group of β carbolines, 6,8 diBr-Norharmano, binds to the dimer of 14-3-3. In the laboratory we are testing interaction through several experimental techniques.