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Rip3 Forms Different Complexes Leading to Apoptosis or Necrosis

We have previously reported (Chen X, Cell Res, 2014 Jan; 24(1):105–210) that MLKL oligomerization leads to translocation of MLKL to lipid rafts of the plasma membrane, and that the plasma membrane MLKL complex acts either by itself or via other proteins to increase sodium influx, which increases osmotic pressure, eventually leading to membrane rupture. Recently, we find that MLKL functions not only as the downstream substrate of Rip3, but also as a regulator of Rip3 status, which would form different complex structures leading to cell survival, apoptosis or necrosis. We also identified some components that block Rip3‐dependent necrosis; these component acts quite differently from GSK872, a kinase inhibitor of Rip3. These compounds effect the interaction between Rip3 and MLKL, leaving Rip3 in a transition state, which delays Rip3‐dependent necrosis and does not induce Rip3‐dependent apoptosis.