Receptor interacting protein (RIP; EC 2.7.11.1) kinases constitute a family of seven members. They are crucial regulators of cell survival and death. Based on sequence similarities, mode of regulation and substrate specificities of their catalytic domain, RIP kinases are closely related to members of the interleukin-1-receptor-associated kinase (IRAK) family. RIP1 and RIP2 (CARDIAK/RICK) also bear a C-terminal domain belonging to the death domain (DD) superfamily, namely, a DD and a caspase recruitment domain (CARD), respectively, allowing recruitment to large protein complexes initiating different signaling pathways. RIP1 is a crucial adaptor kinase on the crossroad of stress-induced signaling pathways (NF-κB, MAPK, Ubiquitin) and a cell's decision to live or die. It is is constitutively expressed in many tissues. However, TNF-α treatment and T-cell activation can also induce RIP1 expression[1].