| Literature DB >> 20471954 |
Flavie Strappazzon1, Sakina Torch, Christine Chatellard-Causse, Anne Petiot, Chantal Thibert, Béatrice Blot, Jean-Marc Verna, Rémy Sadoul.
Abstract
The cytoplasmic protein Alix/AIP1 (ALG-2 interacting protein X) is involved in cell death through mechanisms which remain unclear but require its binding partner ALG-2 (apoptosis-linked gene-2). The latter was defined as a regulator of calcium-induced apoptosis following endoplasmic reticulum (ER) stress. We show here that Alix is also a critical component of caspase 9 activation and apoptosis triggered by calcium. Indeed, expression of Alix dominant-negative mutants or downregulation of Alix afford significant protection against cytosolic calcium elevation following thapsigargin (Tg) treatment. The function of Alix in this paradigm requires its interaction with ALG-2. In addition, we demonstrate that caspase 9 activation is necessary for apoptosis induced by Tg and that this activation is impaired by knocking down Alix. Altogether, our findings identify, for the first time, Alix as a crucial mediator of Ca(2+) induced caspase 9 activation. Copyright (c) 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20471954 DOI： 10.1016/j.bbrc.2010.05.062
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575