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CELL GROWTH AND DEVELOPMENT

Two Adjacent Trimeric Fas Ligands Are Required for Fas Signaling and Formation of a Death-Inducing Signaling Complex

Nils Holler, Aubry Tardivel, Magdalena Kovacsovics-Bankowski, Sylvie Hertig, Olivier Gaide, Fabio Martinon, Antoine Tinel, David Deperthes, Silvio Calderara, Therese Schulthess, Jürgen Engel, Pascal Schneider, Jürg Tschopp
Nils Holler
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Aubry Tardivel
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Magdalena Kovacsovics-Bankowski
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Sylvie Hertig
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Olivier Gaide
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Fabio Martinon
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Antoine Tinel
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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David Deperthes
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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Silvio Calderara
2Apotech Corporation, CH-1066 Epalinges
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Therese Schulthess
3Biozentrum, CH-4000 Basel, Switzerland
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Jürgen Engel
3Biozentrum, CH-4000 Basel, Switzerland
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Pascal Schneider
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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  • For correspondence: pascal.schneider@ib.unil.ch
Jürg Tschopp
1Institute of Biochemistry, BIL Biomedical Research Center, University of Lausanne
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DOI: 10.1128/MCB.23.4.1428-1440.2003
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ABSTRACT

The membrane-bound form of Fas ligand (FasL) signals apoptosis in target cells through engagement of the death receptor Fas, whereas the proteolytically processed, soluble form of FasL does not induce cell death. However, soluble FasL can be rendered active upon cross-linking. Since the minimal extent of oligomerization of FasL that exerts cytotoxicity is unknown, we engineered hexameric proteins containing two trimers of FasL within the same molecule. This was achieved by fusing FasL to the Fc portion of immunoglobulin G1 or to the collagen domain of ACRP30/adiponectin. Trimeric FasL and hexameric FasL both bound to Fas, but only the hexameric forms were highly cytotoxic and competent to signal apoptosis via formation of a death-inducing signaling complex. Three sequential early events in Fas-mediated apoptosis could be dissected, namely, receptor binding, receptor activation, and recruitment of intracellular signaling molecules, each of which occurred independently of the subsequent one. These results demonstrate that the limited oligomerization of FasL, and most likely of some other tumor necrosis factor family ligands such as CD40L, is required for triggering of the signaling pathways.

  • Copyright © 2003 American Society for Microbiology
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Two Adjacent Trimeric Fas Ligands Are Required for Fas Signaling and Formation of a Death-Inducing Signaling Complex
Nils Holler, Aubry Tardivel, Magdalena Kovacsovics-Bankowski, Sylvie Hertig, Olivier Gaide, Fabio Martinon, Antoine Tinel, David Deperthes, Silvio Calderara, Therese Schulthess, Jürgen Engel, Pascal Schneider, Jürg Tschopp
Molecular and Cellular Biology Feb 2003, 23 (4) 1428-1440; DOI: 10.1128/MCB.23.4.1428-1440.2003

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Two Adjacent Trimeric Fas Ligands Are Required for Fas Signaling and Formation of a Death-Inducing Signaling Complex
Nils Holler, Aubry Tardivel, Magdalena Kovacsovics-Bankowski, Sylvie Hertig, Olivier Gaide, Fabio Martinon, Antoine Tinel, David Deperthes, Silvio Calderara, Therese Schulthess, Jürgen Engel, Pascal Schneider, Jürg Tschopp
Molecular and Cellular Biology Feb 2003, 23 (4) 1428-1440; DOI: 10.1128/MCB.23.4.1428-1440.2003
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KEYWORDS

Adaptor Proteins, Signal Transducing
apoptosis
Intercellular Signaling Peptides and Proteins
Membrane Glycoproteins

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