The Lymphotoxin-β Receptor Is Necessary and Sufficient for LIGHT-mediated Apoptosis of Tumor Cells
LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-β receptor (LTβR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT w...
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| Published in | The Journal of biological chemistry Vol. 275; no. 19; pp. 14307 - 14315 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
12.05.2000
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| Subjects | |
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| Abstract | LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-β receptor (LTβR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT were identified by introducing point mutations in the A′ → A“ and D → E loops of LIGHT, which altered binding to LTβR and HveA. One mutant of LIGHT exhibits selective binding to HveA and is inactive triggering cell death in HT29.14s cells or induction of ICAM-1 in fibroblasts. Studies with HveA- or LTβR-specific antibodies further indicated that HveA does not contribute, either cooperatively or by direct signaling, to the death pathway activated by LIGHT. LTβR, not HveA, recruits TNF receptor-associated factor-3 (TRAF3), and LIGHT-induced death is blocked by a dominant negative TRAF3 mutant. Together, these results indicate that TRAF3 recruitment propagates death signals initiated by LIGHT-LTβR interaction and implicates a distinct biological role for LIGHT-HveA system. |
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| AbstractList | LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-beta receptor (LTbetaR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT were identified by introducing point mutations in the A' --> A" and D --> E loops of LIGHT, which altered binding to LTbetaR and HveA. One mutant of LIGHT exhibits selective binding to HveA and is inactive triggering cell death in HT29.14s cells or induction of ICAM-1 in fibroblasts. Studies with HveA- or LTbetaR-specific antibodies further indicated that HveA does not contribute, either cooperatively or by direct signaling, to the death pathway activated by LIGHT. LTbetaR, not HveA, recruits TNF receptor-associated factor-3 (TRAF3), and LIGHT-induced death is blocked by a dominant negative TRAF3 mutant. Together, these results indicate that TRAF3 recruitment propagates death signals initiated by LIGHT-LTbetaR interaction and implicates a distinct biological role for LIGHT-HveA system. LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-β receptor (LTβR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT were identified by introducing point mutations in the A′ → A“ and D → E loops of LIGHT, which altered binding to LTβR and HveA. One mutant of LIGHT exhibits selective binding to HveA and is inactive triggering cell death in HT29.14s cells or induction of ICAM-1 in fibroblasts. Studies with HveA- or LTβR-specific antibodies further indicated that HveA does not contribute, either cooperatively or by direct signaling, to the death pathway activated by LIGHT. LTβR, not HveA, recruits TNF receptor-associated factor-3 (TRAF3), and LIGHT-induced death is blocked by a dominant negative TRAF3 mutant. Together, these results indicate that TRAF3 recruitment propagates death signals initiated by LIGHT-LTβR interaction and implicates a distinct biological role for LIGHT-HveA system. LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-beta receptor (LTbetaR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT were identified by introducing point mutations in the A' --> A" and D --> E loops of LIGHT, which altered binding to LTbetaR and HveA. One mutant of LIGHT exhibits selective binding to HveA and is inactive triggering cell death in HT29.14s cells or induction of ICAM-1 in fibroblasts. Studies with HveA- or LTbetaR-specific antibodies further indicated that HveA does not contribute, either cooperatively or by direct signaling, to the death pathway activated by LIGHT. LTbetaR, not HveA, recruits TNF receptor-associated factor-3 (TRAF3), and LIGHT-induced death is blocked by a dominant negative TRAF3 mutant. Together, these results indicate that TRAF3 recruitment propagates death signals initiated by LIGHT-LTbetaR interaction and implicates a distinct biological role for LIGHT-HveA system.LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-beta receptor (LTbetaR) and the herpesvirus entry mediator (HveA). LIGHT is a homotrimer that activates proapoptotic and integrin-inducing pathways. Receptor binding residues via LIGHT were identified by introducing point mutations in the A' --> A" and D --> E loops of LIGHT, which altered binding to LTbetaR and HveA. One mutant of LIGHT exhibits selective binding to HveA and is inactive triggering cell death in HT29.14s cells or induction of ICAM-1 in fibroblasts. Studies with HveA- or LTbetaR-specific antibodies further indicated that HveA does not contribute, either cooperatively or by direct signaling, to the death pathway activated by LIGHT. LTbetaR, not HveA, recruits TNF receptor-associated factor-3 (TRAF3), and LIGHT-induced death is blocked by a dominant negative TRAF3 mutant. Together, these results indicate that TRAF3 recruitment propagates death signals initiated by LIGHT-LTbetaR interaction and implicates a distinct biological role for LIGHT-HveA system. |
| Author | Rooney, Isabelle A. Benedict, Chris A. Glass, Alison A. Borboroglu, Stephen Cohen, Gary H. Whitbeck, J.Charles Eisenberg, Roselyn J. Butrovich, Kris D. Ware, Carl F. |
| Author_xml | – sequence: 1 givenname: Isabelle A. surname: Rooney fullname: Rooney, Isabelle A. organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 – sequence: 2 givenname: Kris D. surname: Butrovich fullname: Butrovich, Kris D. organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 – sequence: 3 givenname: Alison A. surname: Glass fullname: Glass, Alison A. organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 – sequence: 4 givenname: Stephen surname: Borboroglu fullname: Borboroglu, Stephen organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 – sequence: 5 givenname: Chris A. surname: Benedict fullname: Benedict, Chris A. organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 – sequence: 6 givenname: J.Charles surname: Whitbeck fullname: Whitbeck, J.Charles organization: Department of Microbiology and Center for Oral Health Research, School of Dental Medicine and Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 – sequence: 7 givenname: Gary H. surname: Cohen fullname: Cohen, Gary H. organization: Department of Microbiology and Center for Oral Health Research, School of Dental Medicine and Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 – sequence: 8 givenname: Roselyn J. surname: Eisenberg fullname: Eisenberg, Roselyn J. organization: Department of Microbiology and Center for Oral Health Research, School of Dental Medicine and Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 – sequence: 9 givenname: Carl F. surname: Ware fullname: Ware, Carl F. email: carl_ware@liai.org organization: Division of Molecular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121 |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10799510$$D View this record in MEDLINE/PubMed |
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| Snippet | LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-β receptor (LTβR) and the herpesvirus... LIGHT is a tumor necrosis factor (TNF) ligand superfamily member, which binds two known cellular receptors, lymphotoxin-beta receptor (LTbetaR) and the... |
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| StartPage | 14307 |
| SubjectTerms | Amino Acid Sequence Apoptosis - physiology Base Sequence DNA Primers Humans Integrins - biosynthesis Lymphotoxin beta Receptor Molecular Sequence Data Precipitin Tests Proteins - metabolism Receptors, Tumor Necrosis Factor - chemistry Receptors, Tumor Necrosis Factor - physiology Recombinant Proteins - metabolism Sequence Homology, Amino Acid Signal Transduction Surface Plasmon Resonance TNF Receptor-Associated Factor 3 Tumor Cells, Cultured |
| Title | The Lymphotoxin-β Receptor Is Necessary and Sufficient for LIGHT-mediated Apoptosis of Tumor Cells |
| URI | https://dx.doi.org/10.1074/jbc.275.19.14307 https://www.ncbi.nlm.nih.gov/pubmed/10799510 https://www.proquest.com/docview/71097763 |
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