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Originally published In Press as doi:10.1074/jbc.M207618200 on December 23, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8309-8315, March 7, 2003
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Association of the Death-inducing Signaling Complex with Microdomains after Triggering through CD95/Fas
EVIDENCE FOR CASPASE-8-GANGLIOSIDE INTERACTION IN T CELLS*

Tina Garofalo, Roberta Misasi, Vincenzo Mattei, Anna Maria GiammarioliDagger , Walter MalorniDagger , Giuseppe M. Pontieri, Antonio Pavan§, and Maurizio Sorice

From the Dipartimento di Medicina Sperimentale e Patologia, Università "La Sapienza," Roma, viale Regina Elena 324, 00161 Rome, Italy, the Dagger  Department of Ultrastructures, Istituto Superiore di Sanità, Viale Regina Elena 299, 00161 Rome, Italy, and the § Dipartimento di Medicina Sperimentale, Università di L'Aquila, Via Vetoio Coppito 2, 67100 L'Aquila, Italy

In this investigation we show that the death-inducing signaling complex (DISC) associates with glycosphingolipid-enriched microdomains (GEM) upon CD95/Fas engagement. We primarily analyzed the ganglioside pattern and composition of GEM after triggering through CD95/Fas and observed that GM3 is the main ganglioside constituent of GEM. Stimulation with anti-CD95/Fas did not cause translocation of gangliosides within or from the GEM fraction. Scanning confocal microscopy showed that triggering through CD95/Fas induced a significant GM3-caspase-8 association, as revealed by nearly complete colocalization areas. Coimmunoprecipitation experiments demonstrated that GM3 and GM1 were immunoprecipitated by anti-caspase-8 only after triggering through CD95/Fas. This association was supported by the recruitment of caspase-8, as well as of CD95/Fas, to GEM upon CD95/Fas engagement, as revealed by the analysis of linear sucrose gradient fractions. It indicates that the DISC associates with GEM; no changes were observed in the distribution of caspase-9. The disruption of GEM by methyl-beta -cyclodextrin prevented DNA fragmentation, as well as CD95/Fas clustering on the cell surface, demonstrating a role for GEM in initiating of Fas signaling.

These findings strongly suggest a role for gangliosides as structural components of the membrane multimolecular signaling complex involved in CD95/Fas receptor-mediated apoptotic pathway.

* This work was supported by grants from Ministero dell'Università e della Ricerca Scientifica e Tecnologica (MIUR) and Ateneo 2001.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom all correspondence should be addressed: Dip. Medicina Sperimentale e Patologia, Università "La Sapienza," Roma, viale Regina Elena 324, Roma 00161, Italy. Tel.: 39-6-49972675; Fax: 39-6-4454820; E-mail: maurizio.sorice@uniroma1.it.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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