Science. 1999 Jan 22;283(5401):543-6.

Prevention of constitutive TNF receptor 1 signaling by silencer of death domains.External

Jiang, Y., Woronicz, J. D., Liu, W., Goeddel, D. V.,
--- - Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.
Tumor necrosis factor receptor type 1 (TNF-R1) contains a cytoplasmic death domain that is required for the signaling of TNF activities such as apoptosis and nuclear factor kappa B (NF-kappaB) activation. Normally, these signals are generated only after TNF-induced receptor aggregation. However, TNF-R1 self-associates and signals independently of ligand when overexpressed. This apparent paradox may be explained by silencer of death domains (SODD), a widely expressed approximately 60-kilodalton protein that was found to be associated with the death domain of TNF-R1. TNF treatment released SODD from TNF-R1, permitting the recruitment of proteins such as TRADD and TRAF2 to the active TNF-R1 signaling complex. SODD also interacted with death receptor-3 (DR3), another member of the TNF receptor superfamily. Thus, SODD association may be representative of a general mechanism for preventing spontaneous signaling by death domain-containing receptors.
PMID: 9915703External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vivo interaction
Overexpression DD1 DD2 Reference
Family DD1 DD2 Method Species Region Species Region
DD TNFR1 Link TRADD Co-immunoprecipitation HEK293 Not specified Not specified Not specified Not specified 9915703
(Link: click this icon to show interactions only between the two corresponding DDs)