PMC:3585731 / 31557-34067 JSONTXT

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We examined the effect of Ala and Asp mutants at both sites during necroptosis. In our hands, both Asp mutants displayed activity comparable to wild type Akt, while both Ala mutants displayed comparable decreases in activity (Fig. S8C). Despite similar catalytic activities, Thr308 and Ser473 mutants displayed major differences in their ability to promote necroptotic changes (Fig. 7E,F,G). As expected, the S473D mutant, which was phosphorylated on Thr308 after the addition of zVAD, displayed only slightly reduced activity, while S473A was significantly less active in all aspects of necroptosis. S473A was unable to be efficiently phosphorylated on Thr308 possibly due to the inability of the Ala mutated 473 site to be phosphorylated and provide a docking site for PDK1 to phosphorylate Thr308 [39]. Strikingly, both Ala and Asp mutants of Thr308 were significantly less active in promoting cell death, phosphorylation of JNK and c-Jun, and TNFα mRNA. This suggests that T308D, in spite of being an active Akt construct, may not be a perfect mimic of phosphorylation and this mutant form of the kinase may not have sufficient activity to phosphorylate the entire repertoire of substrates in the cells. When tested, T308D did not support the downstream phosphorylation of several substrates that were phosphorylated by the Myr-Akt construct in the presence of zVAD including FoxO1, Foxo4, MDM2, and p70S6K (Fig. S8D). Our model, based on these results, is that necroptosis-specific Thr308 phosphorylation provides a critical link between necroptotic machinery and Akt kinase, allowing Akt to phosphorylate substrates during necroptosis, promote TNFα synthesis, JNK activation and eventual cell 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