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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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Structure-Based Analysis of the Herpes Simplex Virus Glycoprotein D Binding Site Present on Herpesvirus Entry Mediator HveA (HVEM).
S. A. Connolly, D. J. Landsburg, A. Carfi, D. C. Wiley, R. J. Eisenberg, and G. H. Cohen (2002)
J. Virol.
76, 10894-10904
|Abstract »|Full Text »|PDF »
BLyS and APRIL Form Biologically Active Heterotrimers That Are Expressed in Patients with Systemic Immune-Based Rheumatic Diseases.
V. Roschke, S. Sosnovtseva, C. D. Ward, J. S. Hong, R. Smith, V. Albert, W. Stohl, K. P. Baker, S. Ullrich, B. Nardelli, et al. (2002)
J. Immunol.
169, 4314-4321
|Abstract »|Full Text »|PDF »
Regulation of the Subcellular Localization of Tumor Necrosis Factor Receptor-associated Factor (TRAF)2 by TRAF1 Reveals Mechanisms of TRAF2 Signaling.
J. R. Arron, Y. Pewzner-Jung, M. C. Walsh, T. Kobayashi, and Y. Choi (2002)
J. Exp. Med.
196, 923-934
|Abstract »|Full Text »|PDF »
Seeing the Light: Preassembly and Ligand-Induced Changes of the Interferon {gamma} Receptor Complex in Cells.
C. D. Krause, E. Mei, J. Xie, Y. Jia, M. A. Bopp, R. M. Hochstrasser, and S. Pestka (2002)
Mol. Cell. Proteomics
1, 805-815
|Abstract »|Full Text »|PDF »
CD40, an extracellular receptor for binding and uptake of Hsp70-peptide complexes.
T. Becker, F.-U. Hartl, and F. Wieland (2002)
J. Cell Biol.
158, 1277-1285
|Abstract »|Full Text »|PDF »
Rabies Virus Glycoprotein (RVG) Is a Trimeric Ligand for the N-terminal Cysteine-rich Domain of the Mammalian p75 Neurotrophin Receptor.
C. Langevin, H. Jaaro, S. Bressanelli, M. Fainzilber, and C. Tuffereau (2002)
J. Biol. Chem.
277, 37655-37662
|Abstract »|Full Text »|PDF »
Disabling Receptor Ensembles with Rationally Designed Interface Peptidomimetics.
A. Berezov, J. Chen, Q. Liu, H.-T. Zhang, M. I. Greene, and R. Murali (2002)
J. Biol. Chem.
277, 28330-28339
|Abstract »|Full Text »|PDF »
Cowpox virus encodes a fifth member of the tumor necrosis factor receptor family: A soluble, secreted CD30 homologue.
J. F. Panus, C. A. Smith, C. A. Ray, T. D. Smith, D. D. Patel, and D. J. Pickup (2002)
PNAS
99, 8348-8353
|Abstract »|Full Text »|PDF »
A Fifteen-Amino-Acid TVB Peptide Serves as a Minimal Soluble Receptor for Subgroup B Avian Leukosis and Sarcoma Viruses.
Amyloid beta Binds Trimers as Well as Monomers of the 75-kDa Neurotrophin Receptor and Activates Receptor Signaling.
M. Yaar, S. Zhai, R. E. Fine, P. B. Eisenhauer, B. L. Arble, K. B. Stewart, and B. A. Gilchrest (2002)
J. Biol. Chem.
277, 7720-7725
|Abstract »|Full Text »|PDF »
All TRAFs are not created equal: common and distinct molecular mechanisms of TRAF-mediated signal transduction.
J. Y. Chung, Y. C. Park, H. Ye, and H. Wu (2002)
J. Cell Sci.
115, 679-688
|Abstract »|Full Text »|PDF »
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.
