Anti-RIP

RIP (Receptor Interacting Protein) is a 74 ka Ser/Thr kinase which interacts with CD95 (Fas/APO1) receptor and the tumor necrosis factor receptor (TNFR1). It is a cell death domain adapter protein which can bind to the adapter proteins TRADD, RAID (CRADD) and TRAF2. RIP contains an N terminal region with homology to protein kinases, an intermediate domain capable of association with MAPKKK and a C terminal region containing an intracellular death domain motif. RIP activates both p38 MAP Kinase and SAPK families. In vitro, RIP induces apoptosis, as well as SAPK/JNK and NF-kB activation. NF-kB activation through TRADD, TRAF2 and RIP can be triggered also by DR3/APO3 upon activation with APO3/Tweak ligand. DR4 and DR5 also use FADD, TRADD, and RIP in their signal transduction pathways. RIP deficient mice fail to thrive, displaying extensive apoptosis in both lymphoid and adipose tissues and dying at 1-3 days of age. RIP possesses kinase activity as it autophosphorylates itself on serine and threonine residues. Protein function: Required for vesicle docking or fusion during acrosome biogenesis. May play a role in RNA trafficking or localization. In case of infection by HIV-1, acts as a cofactor for viral Rev and promotes movement of Rev-responsive element- containing RNAs from the nuclear periphery to the cytoplasm. This step is essential for HIV-1 replication. [The UniProt Consortium]