Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family

Mariapia A. Degli-Esposti, Pamela J. Smolak, Henning Walczak, Jennifer Waugh, Chang Pin Huang, Robert F. DuBose, Raymond G. Goodwin, Craig A. Smith

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    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.

    Original languageEnglish
    Pages (from-to)1165-1170
    Number of pages6
    JournalJournal of Experimental Medicine
    Volume186
    Issue number7
    DOIs
    Publication statusPublished - 6 Oct 1997

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    Degli-Esposti, M. A., Smolak, P. J., Walczak, H., Waugh, J., Huang, C. P., DuBose, R. F., ... Smith, C. A. (1997). Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. Journal of Experimental Medicine, 186(7), 1165-1170. https://doi.org/10.1084/jem.186.7.1165