Control of TRAIL-Induced Apoptosis by a Family of Signaling and Decoy Receptors

Author:

Sheridan James P.12,Marsters Scot A.12,Pitti Robert M.12,Gurney Austin12,Skubatch Maya12,Baldwin Daryl12,Ramakrishnan Lakshmi12,Gray Christa L.12,Baker Kevin12,Wood William I.12,Goddard Audrey D.12,Godowski Paul12,Ashkenazi Avi12

Affiliation:

1. J. P. Sheridan, S. A. Marsters, R. M. Pitti, M. Skubatch, A. Ashkenazi, Department of Molecular Oncology, Genentech, South San Francisco, CA 94080–4918, USA.

2. A. Gurney, D. Baldwin, L. Ramakrishnan, C. L. Gray, K. Baker, W. I. Wood, A. D. Goddard, P. Godowski, Department of Molecular Biology, Genentech, South San Francisco, CA 94080–4918, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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