Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

The overall goal of this methodology is to visualize one of the first steps in the activation of an initiator caspases. This step is called induced proximity and occurs when caspase molecules come together to form active dimers during apoptotic cell death. This method can help answer key questions in the caspase field such as when, where, and how efficiently specific initiator caspases can get be activated.

The main advantage of this technique is that one can visualize the assembly of caspase activation complexes in living cells in real time. This biomolecular fluorescence complementation method uses fragments of the thyroxine protein, Venus, that have infused to a caspase. The fragments are not fluorescent on their own but when the caspase undergoes induced proximity, this brings the two Venus halves together and they light up.