Control of TRAIL-Induced Apoptosis by a Family of Signaling and Decoy Receptors
James P. Sheridan(Johnson & Johnson (United States)), Scot A. Marsters(Johnson & Johnson (United States)), Robert Pitti(Johnson & Johnson (United States)), Austin Gurney(Johnson & Johnson (United States)), Maya Skubatch(Johnson & Johnson (United States)), Daryl T. Baldwin(Johnson & Johnson (United States)), Lakshmi Ramakrishnan(Johnson & Johnson (United States)), Christa L. Gray(Johnson & Johnson (United States)), Kevin P. Baker(Johnson & Johnson (United States)), William I. Wood(Johnson & Johnson (United States)), Audrey D. Goddard(Johnson & Johnson (United States)), Paul J. Godowski(Johnson & Johnson (United States)), Avi Ashkenazi(Johnson & Johnson (United States))
Cited by 1,669
Abstract
TRAIL (also called Apo2L) belongs to the tumor necrosis factor family, activates rapid apoptosis in tumor cells, and binds to the death-signaling receptor DR4. Two additional TRAIL receptors were identified. The receptor designated death receptor 5 (DR5) contained a cytoplasmic death domain and induced apoptosis much like DR4. The receptor designated decoy receptor 1 (DcR1) displayed properties of a glycophospholipid-anchored cell surface protein. DcR1 acted as a decoy receptor that inhibited TRAIL signaling. Thus, a cell surface mechanism exists for the regulation of cellular responsiveness to pro-apoptotic stimuli.
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