Our research is focused on the study of dynamic membrane processes from a quantitative point of view. We have a special interest in the mitochondrial membrane alterations during apoptosis and the mechanism of action of the Bcl-2 proteins. To address these problems, we make use of our expertise in membrane biophysics, advanced microscopy and single molecule techniques.
The proteins of the Bcl-2 family are essential regulators of apoptosis. They control a key event in apoptosis: the permeabilization of the mitochondrial outer membrane (MOM) that leads to the activation of caspases and to cell death. Because the Bcl-2 proteins have an important role in the formation of tumors and in the cellular responses to anti-cancer therapies, understanding the molecular details of their action is of great therapeutic interest.
We apply fluorescence correlation spectroscopy, atomic force microscopy and single particle tracking to in vitro reconstituted systems in order to characterize the complex interaction networks between the members of the Bcl-2 proteins. Our strategy includes approaches to clarify the role of the mitochondrial membrane, which strongly influences the molecular mechanism of these proteins. Our desire is to use the quantitative insight provided by advanced microscopy and single molecule techniques to build a mathematical model for the mitochondrial pathway of apoptosis.