Cloning and Characterization of TRAIL-R3, a Novel Member of the Emerging TRAIL Receptor Family
Open Access
- 6 October 1997
- journal article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 186 (7) , 1165-1170
- https://doi.org/10.1084/jem.186.7.1165
Abstract
TRAIL-R3, a new member of the TRAIL receptor family, has been cloned and characterized. TRAIL-R3 encodes a 299 amino acid protein with 58 and 54% overall identity to TRAIL-R1 and -R2, respectively. Transient expression and quantitative binding studies show TRAIL-R3 to be a plasma membrane–bound protein capable of high affinity interaction with the TRAIL ligand. The TRAIL-R3 gene maps to human chromosome 8p22-21, clustered with the genes encoding two other TRAIL receptors. In contrast to TRAIL-R1 and -R2, this receptor shows restricted expression, with transcripts detectable only in peripheral blood lymphocytes and spleen. The structure of TRAIL-R3 is unique when compared to the other TRAIL receptors in that it lacks a cytoplasmic domain and appears to be glycosyl-phosphatidylinositol–linked. Moreover, unlike TRAIL-R1 and -R2, in a transient overexpression system TRAIL-R3 does not induce apoptosis.Keywords
This publication has 29 references indexed in Scilit:
- CAR1, a TNFR–Related Protein, Is a Cellular Receptor for Cytopathic Avian Leukosis–Sarcoma Viruses and Mediates ApoptosisCell, 1996
- Identification and characterization of a new member of the TNF family that induces apoptosisImmunity, 1995
- Fas Ligand-Induced Apoptosis as a Mechanism of Immune PrivilegeScience, 1995
- The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activationCell, 1995
- The TNF receptor superfamily of cellular and viral proteins: Activation, costimulation, and deathCell, 1994
- A family of ligands for the TNF receptor superfamilyThe International Journal of Cell Cloning, 1994
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- Stimulation of human Jurkat cells by monoclonal antibody crosslinking of transfected-Ly-6A.2 (TAP) moleculesCellular Immunology, 1991
- The Immunoglobulin Superfamily—Domains for Cell Surface RecognitionAnnual Review of Immunology, 1988
- Demonstration of phosphatidylinositol anchors on Ly-6 molecules by specific phospholipase C digestion and gel electrophoresis in octylglucosideBiochemical and Biophysical Research Communications, 1987