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Molecular and Cellular Biology, August 2005, p. 6811-6820, Vol. 25, No. 15
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.15.6811-6820.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Amplification of Fas-Mediated Apoptosis in Type II Cells via Microdomain Recruitment

Laboratoire CIRID, CNRS UMR 5164, Université de Bordeaux 2, 146 rue Léo Saignat, Bordeaux 33076, France,¹ Laboratoire de Biogenèse Membranaire, CNRS UMR 5200, Université de Bordeaux 2, 146 rue Léo Saignat, Bordeaux 33076, France,² Centre de Lutte Contre le Cancer Bergonié et Institut Européen de Chimie et Biologie, 33600 Pessac, France³

Received 4 February 2005/ Returned for modification 21 March 2005/ Accepted 26 April 2005

Fas triggers apoptosis via the caspase cascade when bound to its ligand FasL. In type I cells, Fas is concentrated into the plasma membrane lipid rafts, and these domains are required for the apoptotic signal to occur. In contrast, Fas is excluded from the microdomains in type II cells. We report that the coligation with Fas of the membrane receptor CD28 strongly increases Fas-induced apoptosis in type II T lymphocytes, whereas it has no effect in a type I cell line. The effect of CD28 is independent of its intracellular region and requires the recruitment of the microdomains. Indeed, upon CD28 costimulation, Fas is redistributed in the lipid rafts, and their disruption with a cholesterol chelator abrogates the effect of CD28. The microdomain-mediated cell death amplification does not alter death-induced signaling complex formation and is mediated by the enhancement of the mitochondrial apoptotic pathway. These findings indicate that the sensitivity to Fas-induced apoptosis of type II cells can be amplified in vivo by the recruitment of lipid rafts following interactions between nonapoptotic ligand/receptor pairs during cell-to-cell contacts.

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