The interests of my laboratory is focussed in the study of the structure/function relationships of proteins involved in several pathologies, mainly those related to methionine metabolism. For this purpose, we used in vitro and in vivo techniques that allow detection of changes in folding, association, interactions, subcelular localization, activity or regulation of these enzymes. To date, we have identified from key active site residues, to post-translational modifications involved in the control of oligomerization processes or folding intermediates.
Recently, we demonstrated expression of some enzymes of this pathway (MAT I/III) in many tissues where their existence was unknown. Additionally, in those tissues with low expression surprisingly the proteins localize to the nucleus, instead to the cytoplasm that was consider their exclusive location. Moreover, we have been able to map the areas involved in both cytoplasmic retention and nuclear loacalization, as well as to demonstrate that nuclear accumulation correlates with increases in specific epigenetic modifications. Now, we are centered in the study of the mechanisms that control these processes and their putative pathological alterations.