Phosphorylation of FADD/ MORT1 at Serine 194 and Association with a 70-kDa Cell Cycle-Regulated Protein Kinase
作者： Carsten Scaffidi , Jörg Volkland , Ida Blomberg , Ingrid Hoffmann , Peter H. Krammer
DOI: 10.4049/JIMMUNOL.164.3.1236
关键词:
摘要: The adapter molecule Fas-associated death domain protein (FADD)/mediator of receptor-induced toxicity-1 (MORT1) is essential for signal transduction the apoptosis-inducing receptor CD95 (APO-1/Fas) as it connects activated with effector caspase-8. FADD also plays a role in embryonic development and cell cycle reentry T cells. phosphorylated at serine residues. We now show that phosphorylation exclusively occurs 194. was found to correlate cycle. In cells arrested G2/M boundary nocodazole, quantitatively phosphorylated, whereas only nonphosphorylated G1/S hydroxyurea. this context, we have identified 70-kDa cycle-regulated kinase specifically binds C-terminal half FADD. Because CD95-mediated apoptosis independent cycle, may regulate its apoptosis-independent functions.
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