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))
Science
August 8, 1997
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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