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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Alix and ALG-2 are involved in tumor necrosis factor receptor 1-induced cell death.

Alix/AIP1 regulates cell death in a way involving interactions with the calcium-binding protein ALG-2 and with proteins of ESCRT (endosomal sorting complex required for transport). Using mass spectrometry we identified caspase-8 among proteins co-immunoprecipitating with Alix in dying neurons. We next demonstrated that Alix and ALG-2 interact with pro-caspase-8 and that Alix forms a complex with the TNFalpha receptor-1 (TNF-R1), depending on its capacity to bind ESCRT proteins. Thus, Alix and ALG-2 may allow the recruitment of pro-caspase-8 onto endosomes containing TNF-R1, a step thought to be necessary for activation of the apical caspase. In line with this, expression of Alix deleted of its ALG-2-binding site (AlixDeltaALG-2) significantly reduced TNF-R1-induced cell death, without affecting endocytosis of the receptor. In a more physiological setting, we found that programmed cell death of motoneurons, which can be inhibited by AlixDeltaALG-2, is regulated by TNF-R1. Taken together, these results highlight Alix and ALG-2 as new actors of the TNF-R1 pathway.[1]

References

  1. Alix and ALG-2 are involved in tumor necrosis factor receptor 1-induced cell death. Mahul-Mellier, A.L., Strappazzon, F., Petiot, A., Chatellard-Causse, C., Torch, S., Blot, B., Freeman, K., Kuhn, L., Garin, J., Verna, J.M., Fraboulet, S., Sadoul, R. J. Biol. Chem. (2008) [Pubmed]
 
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