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

Autor: Sakina Torch, Rémy Sadoul, Jérôme Garin, Christine Chatellard-Causse, Béatrice Blot, Anne Petiot, Kimberley Freeman, Flavie Strappazzon, Jean Marc Verna, Sandrine Fraboulet, Loriane Kuhn, Anne-Laure Mahul-Mellier
Přispěvatelé: Fraboulet, Sandrine, Grenoble Institut des Neurosciences (GIN), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Collaboration
Jazyk: angličtina
Rok vydání: 2008
Předmět:
MESH: Cell Death
MESH: Neurons
Cell Cycle Proteins
Chick Embryo
MESH: Calcium-Binding Proteins
Biochemistry
MESH: Caspase 8
MESH: Recombinant Proteins
MESH: Protein Structure
Tertiary

0302 clinical medicine
Calcium-binding protein
MESH: Animals
Caspase
Neurons
MESH: Receptors
Tumor Necrosis Factor
Type I

Caspase 8
0303 health sciences
Cell Death
biology
MESH: Chick Embryo
Endocytosis
Recombinant Proteins
Cell biology
Neural Crest
Receptors
Tumor Necrosis Factor
Type I

030220 oncology & carcinogenesis
MESH: Endocytosis
Endosome
Endosomes
ESCRT
03 medical and health sciences
Molecular Basis of Cell and Developmental Biology
MESH: Cell Cycle Proteins
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology

Animals
Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology

Cell Cycle Protein
Molecular Biology
030304 developmental biology
Binding Sites
MESH: Humans
Endosomal Sorting Complexes Required for Transport
MESH: Apoptosis Regulatory Proteins
Calcium-Binding Proteins
Cell Biology
MESH: Neural Crest
Protein Structure
Tertiary

MESH: Binding Sites
MESH: Endosomes
biology.protein
Tumor necrosis factor receptor 1
Apoptosis Regulatory Proteins
Zdroj: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2008, 283 (50), pp.34954-65. ⟨10.1074/jbc.M803140200⟩
Journal of Biological Chemistry, 2008, 283 (50), pp.34954-65. ⟨10.1074/jbc.M803140200⟩
ISSN: 0021-9258
1083-351X
DOI: 10.1074/jbc.M803140200⟩
Popis: International audience; 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.
Databáze: OpenAIRE