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A Domain in TNF Receptors That Mediates Ligand-Independent Receptor Assembly and Signaling
Francis Ka-Ming Chan,
Hyung J. Chun,
Lixin Zheng,
Richard M. Siegel,
Kimmie L. Bui,*
Michael J. Lenardo
A conserved domain in the extracellular region of the 60- and
80-kilodalton tumor necrosis factor receptors (TNFRs) was
identifiedthat mediates specific ligand-independent assembly of
receptortrimers. This pre-ligand-binding assembly domain (PLAD) is
physicallydistinct from the domain that forms the major contacts with
ligand,but is necessary and sufficient for the assembly of TNFR
complexesthat bind TNF- and mediate signaling. Other members of the
TNFRsuperfamily, including TRAIL receptor 1 and CD40, show similarhomotypic association. Thus, TNFRs and related receptors appearto
function as preformed complexes rather than as individual receptorsubunits that oligomerize after ligand binding.
Laboratory of Immunology, National Institute of Allergy and
Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
*
Present address: George Washington University School of
Medicine, Washington, DC 20037, USA.
To whom correspondence should be addressed. E-mail:
Lenardo{at}nih.gov
The editors suggest the following Related Resources on Science sites:
In Science Magazine
PERSPECTIVES
Pierre Golstein (30 June 2000) Science288 (5475), 2328.
[DOI: 10.1126/science.288.5475.2328] |Summary »|Full Text »
REPORTS
Richard M. Siegel, John K. Frederiksen, David A. Zacharias, Francis Ka-Ming Chan, Michele Johnson, David Lynch, Roger Y. Tsien, and Michael J. Lenardo (30 June 2000) Science288 (5475), 2354.
[DOI: 10.1126/science.288.5475.2354] |Abstract »|Full Text »|PDF »
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Wall-Associated Kinases Are Expressed throughout Plant Development and Are Required for Cell Expansion.
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Proteases for Cell Suicide: Functions and Regulation of Caspases.
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Fas Preassociation Required for Apoptosis Signaling and Dominant Inhibition by Pathogenic Mutations.
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Science
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Measurement of Molecular Interactions in Living Cells by Fluorescence Resonance Energy Transfer Between Variants of the Green Fluorescent Protein.
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Evidence for Heterotypic Interaction between the Receptor Tyrosine Kinases TIE-1 and TIE-2.
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Characterization of a p75NTR Apoptotic Signaling Pathway Using a Novel Cellular Model.
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and mediate signaling. Other members of the
TNFR superfamily, including TRAIL receptor 1 and CD40, show similar homotypic association. Thus, TNFRs and related receptors appear to
function as preformed complexes rather than as individual receptor subunits that oligomerize after ligand binding.
