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Fas Preassociation Required for Apoptosis Signaling and Dominant Inhibition by Pathogenic Mutations
Richard M. Siegel,1
John K. Frederiksen,1
David A. Zacharias,2
Francis Ka-Ming Chan,1
Michele Johnson,1
David Lynch,3
Roger Y. Tsien,2
Michael J. Lenardo1*
Heterozygous mutations encoding abnormal forms of the
death receptor Fas dominantly interfere with Fas-induced lymphocyteapoptosis in human autoimmune lymphoproliferative syndrome. Thiseffect, rather than depending on ligand-induced receptor
oligomerization,was found to stem from ligand- independent
interaction of wild-typeand mutant Fas receptors through a specific
region in the extracellulardomain. Preassociated Fas complexes were
found in living cellsby means of fluorescence resonance energy
transfer between variantsof green fluorescent protein. These results
show that formationof preassociated receptor complexes is necessary
for Fas signalingand dominant interference in human disease.
1 Laboratory of Immunology, National Institute
of Allergy and Infectious Diseases, National Institutes of Health,
Bethesda, MD 20892, USA.
2 Howard Hughes Medical
Institute and Department of Pharmacology, University of California, San
Diego School of Medicine, La Jolla, CA 92093, USA.
3 Immunex Corporation, 51 University Street,
Seattle, WA 98101, USA.
*
To whom correspondence should be addressed. E-mail:
lenardo{at}nih.gov
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In Science Magazine
PERSPECTIVES
Pierre Golstein (30 June 2000) Science288 (5475), 2328.
[DOI: 10.1126/science.288.5475.2328] |Summary »|Full Text »
REPORTS
Francis Ka-Ming Chan, Hyung J. Chun, Lixin Zheng, Richard M. Siegel, Kimmie L. Bui, and Michael J. Lenardo (30 June 2000) Science288 (5475), 2351.
[DOI: 10.1126/science.288.5475.2351] |Abstract »|Full Text »|PDF »
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Localization of the gD-Binding Region of the Human Herpes Simplex Virus Receptor, HveA.
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A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling.
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Science
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Characterization of a p75NTR Apoptotic Signaling Pathway Using a Novel Cellular Model.
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The p75 Neurotrophin Receptor Activates Akt (Protein Kinase B) through a Phosphatidylinositol 3-Kinase-dependent Pathway.
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