PMC:3585731 / 42882-45183
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Interestingly, we observed phosphorylation of Akt by recombinant RIP1 kinase in vitro on Thr146, 195/197, and 435 and Ser381 residues. Furthermore, mutating these residues to Ala in Myr-Akt leads to the loss of its ability to promote necroptosis. However, we were not able to confirm phosphorylation of these residues on endogenous Akt in L929 cells using either mass spectrometry or western blotting with a phospho-specific antibody raised against Thr435 peptide, suggesting that direct phosphorylation of Akt by RIP1 likely represents an in vitro artifact and does not reflect endogenous regulation. Second, what are the key substrates of Akt that promote necrotic death and TNFα synthesis? On the one hand, our data suggest new roles for Akt effector pathways mediated by mTORC1 in necroptotic control. On the other hand, we have observed only modest changes in mTORC1 activity under necroptotic conditions, suggesting that additional Akt substrates are likely to be involved. This warrants a re-evaluation of the roles of additional Akt substrates in necroptotic death, since no such connections have been established. Similarly, the mechanisms connecting mTORC1 to JNK remain to be elucidated. While there are some recent examples of mTORC1-dependent regulation of JNK, e.g. following ER stress [46], the exact mechanisms during necroptosis remain to be established. Given the activation of JNK by TNFα and the importance of mTORC1-dependent translational control in necroptosis, one possibility is that mTORC1 contributes to the translation of TNFα and forms a positive feed forward loop with 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