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Molecular and Cellular Biology, November 2003, p. 8334-8344, Vol. 23, No. 22
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.22.8334-8344.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

TRUSS, a Novel Tumor Necrosis Factor Receptor 1 Scaffolding Protein That Mediates Activation of the Transcription Factor NF-{kappa}B

Surinder M. Soond,1 Jennifer L. Terry,2 Jeff D. Colbert,2 and David W. H. Riches1,2,3*

Program in Cell Biology, Department of Pediatrics, National Jewish Medical and Research Center, Denver, Colorado 80206,1 Department of Immunology,2 Division of Pulmonary and Critical Care Medicine, Department of Medicine and Department of Pharmacology, University of Colorado Health Sciences Center, Denver, Colorado 802623

Received 8 November 2002/ Returned for modification 20 December 2002/ Accepted 12 August 2003

We describe the cloning and characterization of tumor necrosis factor receptor (TNF-R)-associated ubiquitous scaffolding and signaling protein (TRUSS), a novel TNF-R1-interacting protein of 90.7 kDa. TRUSS mRNA was ubiquitously expressed in mouse tissues but was enriched in heart, liver, and testis. Coimmunoprecipitation experiments showed that TRUSS was constitutively associated with unligated TNF-R1 and that the complex was relatively insensitive to stimulation with TNF-{alpha}. Deletion mutagenesis of TNF-R1 indicated that TRUSS interacts with both the membrane-proximal region and the death domain of TNF-R1. In addition, the N-terminal region of TRUSS (residues 1 to 440) contains sequences that permit association with the cytoplasmic domain of TNF-R1. Transient overexpression of TRUSS activated NF-{kappa}B and increased NF-{kappa}B activation in response to ligation of TNF-R1. In contrast, a COOH-terminal-deletion mutant of TRUSS (TRUSS1-723) was found to inhibit NF-{kappa}B activation by TNF-{alpha}. Coprecipitation and coimmunoprecipitation assays revealed that TRUSS can interact with TRADD, TRAF2, and components of the IKK complex. These findings suggest that TRUSS may serve as a scaffolding protein that interacts with TNF-R1 signaling proteins and may link TNF-R1 to the activation of IKK.

* Corresponding author. Mailing address: Program in Cell Biology, Department of Pediatrics, National Jewish Medical and Research Center, Neustadt Room D405, 1400 Jackson St., Denver, CO 80206. Phone: (303) 398-1188. Fax: (303) 398-1381. E-mail: richesd{at}njc.org.

Molecular and Cellular Biology, November 2003, p. 8334-8344, Vol. 23, No. 22
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.22.8334-8344.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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