ArticleBiochemistry2010
TNF receptor-1 (TNF-R1) ubiquitous scaffolding and signaling protein interacts with TNF-R1 and TRAF2 via an N-terminal docking interface.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Bubbling cell death: A hot air balloon released from the nucleus in the cold.Experimental biology and medicine (Maywood, N.J.) · 2016Review
- UV irradiation/cold shock-mediated apoptosis is switched to bubbling cell death at low temperatures.Oncotarget · 2015Article
- TNF-α induces matrix metalloproteinase-9-dependent soluble intercellular adhesion molecule-1 release via TRAF2-mediated MAPKs and NF-κB activation in osteoblast-like MC3T3-E1 cells.Journal of biomedical science · 2014Article
- Use of chemical probes to detect mitochondrial ROS by flow cytometry and spectrofluorometry.Methods in enzymology · 2014Article
- Role of WWOX and NF-κB in lung cancer progression.Translational respiratory medicine · 2013Review
- TRAF molecules in cell signaling and in human diseases.Journal of molecular signaling · 2013Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
TNF receptor-1 (TNF-R1) signal transduction is mediated through the assembly of scaffolding proteins, adaptors, and kinases. TNF receptor ubiquitous scaffolding and signaling protein (TRUSS), a 90.1 kDa TNF-R1-associated scaffolding protein, also interacts with TRAF2 and IKK and contributes to TNF-alpha-induced nuclear factor-kappaB (NF-kappaB) and c-Jun-NH(2)-terminal kinase (JNK) activation. Little is known about the mechanism of interaction among TRUSS, TNF-R1, and TRAF2. To address this issue, we used deletional and site-directed mutagenesis approaches to systematically investigate (i) the regions of TRUSS that interact with TNF-R1 and TRAF2 and (ii) the ability of TRUSS to self-associate to form higher-order complexes. Here we show that sequences located in the N-terminal (residues 1-248) and central (residues 249-440) regions of TRUSS are required to form a docking interface that supports binding to both TNF-R1 and TRAF2. While the C-terminal region (residues 441-797) did not directly interact with TNF-R1 or TRAF2, sequences located in this region were capable of self-association. Collectively, these data suggest that (i) the interaction between TNF-R1 and TRAF2 requires sequences located in the entire N-terminal half (residues 1-440) of TRUSS, (ii) the binding interface for TNF-R1 is closely linked with the TRAF2 binding interface, and (iii) the assembly of homomeric TRUSS complexes may contribute to its role in TNF-R1 signaling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.