CHARACTERIZATION OF 2 RECEPTORS FOR TRAIL

Two receptors for TRAIL, designated TRAIL-R2 and TRAIL-R3, have been i dentified, Both are members of the tumor necrosis factor receptor fami ly, TRAIL-R2 is structurally similar to the death-domain-containing re ceptor TRAIL-RI (DR-4), and is capable of inducing apoptosis, In contr ast, TRAIL-R3 does not promote cell death, TRAIL-R3 is highly glycosyl ated and is membrane bound via a putative phosphatidylinositol anchor, The extended structure of TRAIL-R3 is due to the presence of multiple threonine-, alanine-, proline-and glutamine-rich repeats (TAPE repeat s), TRAIL-R2 shows a broad tissue distribution, whereas the expression of TRAIL-R3 is restricted to peripheral blood lymphocytes (PBLs) and skeletal muscle, All three TRAIL receptors bind TRAIL with similar aff inity, suggesting a complex regulation of TRAIL-mediated signals. (C) 1997 Federation of European Biochemical Societies.