%0 Journal Article %T Alix and ALG-2 make a link between endosomes and neuronal death. %+ Grenoble Institut des Neurosciences (GIN) %A Mahul-Mellier, Anne-Laure %A Strappazzon, Flavie %A Chatellard-Causse, Christine %A Blot, Béatrice %A Béal, David %A Torch, Sakina %A Hemming, Fiona, J. %A Petiot, Anne %A Verna, Jean-Marc %A Fraboulet, Sandrine %A Sadoul, Rémy %Z This work was supported in part by Inserm, the University Joseph Fourier, grants from the Association Franc¸ aise contre les Myopathies [grant number MNM 2007], the Association pour la Recherche sur la Scle' rose Late' rale Amyotrophique [grant number 060711] and the Association pour la Recherche contre le Cancer [grant number 4948]. A.-L.M.-M. was supported by a fellowship from the Association Franc¸ aise contre les Myopathies. %< avec comité de lecture %@ 0300-5127 %J Biochemical Society Transactions %I Portland Press %V 37 %N Pt 1 %P 200-3 %8 2009-02 %D 2009 %R 10.1042/BST0370200 %M 19143631 %K tumour necrosis factor α receptor 1 (TNFR1) %K apoptosis %K calcium %K caspase %K endosomal sorting complex required for transport (ESCRT) %K neuron %K tumour necrosis factor α receptor 1 (TNFR1). %Z Life Sciences [q-bio]/Biochemistry, Molecular BiologyJournal articles %X Alix [ALG-2 (apoptosis-linked gene 2)-interacting protein X] is a ubiquitinous adaptor protein first described for its capacity to bind to the calcium-binding protein, ALG-2. Alix regulates neuronal death in ways involving interactions with ALG-2 and with proteins of the ESCRT (endosomal sorting complex required for transport). Even though all Alix interactors characterized to date are involved in endosomal trafficking, the genuine function of the protein in this process remains unclear. We have demonstrated recently that Alix and ALG-2 form in the presence of calcium, a complex with apical caspases and with the endocytosed death receptor TNFR1 (tumour necrosis factor alpha receptor 1), thus suggesting a molecular coupling between endosomes and the cell death machinery. %G English %2 https://inserm.hal.science/inserm-00381793/document %2 https://inserm.hal.science/inserm-00381793/file/Mahul_Mellier_et_al._2009.pdf %L inserm-00381793 %U https://inserm.hal.science/inserm-00381793 %~ INSERM %~ UGA %~ UNIV-GRENOBLE1 %~ U836